TY  - JOUR
AU  - Vujčić, Miroslava
AU  - Lazić, Milan
AU  - Milenković, Milica R.
AU  - Sladić, Dušan
AU  - Radulović, Siniša
AU  - Filipović, Nenad R.
AU  - Anđelković, Katarina K.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1168
AB  - Organometallic Cd(II) compounds have recently attracted attention for their anticancer activity. The interaction of the dinuclear complex of Cd(II) with the condensation product of 2-acetylpyridine and malonic acid dihydrazide, N',N'(2)-bis[(1E)-1-(2pyridyl) ethylidene] propanedihydrazide (Cd(II)H(2)L), with calf thymus DNA (CT-DNA) was monitored by blue shift in UV-vis spectra of the complex. The binding constant of Cd(II) H2L complex with CT-DNA was determined (K(B) = 1.8 x 10(4) M(-1)) and was indicative of minor groove binding. Agarose gel electrophoretic changes in mobility of supercoiled and circular forms of pBR322 and pUC18 plasmids in the presence of the complex suggest that conformational changes in the plasmids occur upon binding of the Cd(II) H2L complex. The Cd(II) H2L complex induced perturbation of the cell cycle phase distribution and an increase in the percentage of cells in the sub-G1 phase of human cervical cancer HeLa cell line and murine melanoma B16 cell line. Immunoblotting analysis showed the overexpression of Bcl-2 protein with the Cd(II)H(2)L complex. (C) 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25: 175-182, 2011; View this article online at wileyonlinelibrary.com. DOI 10:1002/jbt.20374
PB  - Wiley-Blackwell, Malden
T2  - Journal of Biochemical and Molecular Toxicology
T1  - A Comparative Study of DNA Binding and Cell Cycle Phase Perturbation by the Dinuclear Complex of Cd(II) with the Condensation Product of 2-Acetylpyridine and Malonic Acid Dihydrazide N ',N ' 2-bis[(1E)-1-(2-pyridyl) ethylidene] propanedihydrazide
VL  - 25
IS  - 3
SP  - 175
EP  - 182
DO  - 10.1002/jbt.20374
ER  - 

@article{
author = "Vujčić, Miroslava and Lazić, Milan and Milenković, Milica R. and Sladić, Dušan and Radulović, Siniša and Filipović, Nenad R. and Anđelković, Katarina K.",
year = "2011",
abstract = "Organometallic Cd(II) compounds have recently attracted attention for their anticancer activity. The interaction of the dinuclear complex of Cd(II) with the condensation product of 2-acetylpyridine and malonic acid dihydrazide, N',N'(2)-bis[(1E)-1-(2pyridyl) ethylidene] propanedihydrazide (Cd(II)H(2)L), with calf thymus DNA (CT-DNA) was monitored by blue shift in UV-vis spectra of the complex. The binding constant of Cd(II) H2L complex with CT-DNA was determined (K(B) = 1.8 x 10(4) M(-1)) and was indicative of minor groove binding. Agarose gel electrophoretic changes in mobility of supercoiled and circular forms of pBR322 and pUC18 plasmids in the presence of the complex suggest that conformational changes in the plasmids occur upon binding of the Cd(II) H2L complex. The Cd(II) H2L complex induced perturbation of the cell cycle phase distribution and an increase in the percentage of cells in the sub-G1 phase of human cervical cancer HeLa cell line and murine melanoma B16 cell line. Immunoblotting analysis showed the overexpression of Bcl-2 protein with the Cd(II)H(2)L complex. (C) 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25: 175-182, 2011; View this article online at wileyonlinelibrary.com. DOI 10:1002/jbt.20374",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of Biochemical and Molecular Toxicology",
title = "A Comparative Study of DNA Binding and Cell Cycle Phase Perturbation by the Dinuclear Complex of Cd(II) with the Condensation Product of 2-Acetylpyridine and Malonic Acid Dihydrazide N ',N ' 2-bis[(1E)-1-(2-pyridyl) ethylidene] propanedihydrazide",
volume = "25",
number = "3",
pages = "175-182",
doi = "10.1002/jbt.20374"
}

Vujčić, M., Lazić, M., Milenković, M. R., Sladić, D., Radulović, S., Filipović, N. R.,& Anđelković, K. K.. (2011). A Comparative Study of DNA Binding and Cell Cycle Phase Perturbation by the Dinuclear Complex of Cd(II) with the Condensation Product of 2-Acetylpyridine and Malonic Acid Dihydrazide N ',N ' 2-bis[(1E)-1-(2-pyridyl) ethylidene] propanedihydrazide. in Journal of Biochemical and Molecular Toxicology
Wiley-Blackwell, Malden., 25(3), 175-182.
https://doi.org/10.1002/jbt.20374

Vujčić M, Lazić M, Milenković MR, Sladić D, Radulović S, Filipović NR, Anđelković KK. A Comparative Study of DNA Binding and Cell Cycle Phase Perturbation by the Dinuclear Complex of Cd(II) with the Condensation Product of 2-Acetylpyridine and Malonic Acid Dihydrazide N ',N ' 2-bis[(1E)-1-(2-pyridyl) ethylidene] propanedihydrazide. in Journal of Biochemical and Molecular Toxicology. 2011;25(3):175-182.
doi:10.1002/jbt.20374 .

Vujčić, Miroslava, Lazić, Milan, Milenković, Milica R., Sladić, Dušan, Radulović, Siniša, Filipović, Nenad R., Anđelković, Katarina K., "A Comparative Study of DNA Binding and Cell Cycle Phase Perturbation by the Dinuclear Complex of Cd(II) with the Condensation Product of 2-Acetylpyridine and Malonic Acid Dihydrazide N ',N ' 2-bis[(1E)-1-(2-pyridyl) ethylidene] propanedihydrazide" in Journal of Biochemical and Molecular Toxicology, 25, no. 3 (2011):175-182,
https://doi.org/10.1002/jbt.20374 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Ruiz, Jordi
AU  - Lopez-Santin, Josep
AU  - Vujčić, Zoran
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1151
AB  - Highly efficient raw starch digesting alpha-amylase was produced after 24 h of batch fermentation of Bacillus licheniformis ATCC 9945a in laboratory bioreactor at 37 degrees C. The enzyme was purified by gel filtration chromatographies with 6-fold increase of specific activity and 38% recovery and showed a molecular mass of 31 kDa by SDS-PAGE. The purified enzyme had an optimum pH of 6.5 and optimum temperature of 90 degrees C. The purified alpha-amylase in the presence of CaCl(2) retained 55% of its activity after 6 h of incubation at 70 degrees C. Co(2+), Ni(2+) and Ca(2+) slightly stimulated, while Hg(2+) completely inhibited alpha-amylase activity. Hydrolysis rates of raw triticale, wheat, potato, horseradish and corn starches, at 1% concentration were 63, 60, 59, 52 and 37%, respectively, in a period of 4 h. The properties of the purified enzyme proved its high efficacy for digesting diverse raw starches below gelatinization temperature and, hence, its potential commercial value to use as an industrial enzyme. (C) 2010 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Sa, Lausanne
T2  - Biochemical Engineering Journal
T1  - Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a
VL  - 53
IS  - 2
SP  - 203
EP  - 209
DO  - 10.1016/j.bej.2010.10.014
ER  - 

@article{
author = "Božić, Nataša and Ruiz, Jordi and Lopez-Santin, Josep and Vujčić, Zoran",
year = "2011",
abstract = "Highly efficient raw starch digesting alpha-amylase was produced after 24 h of batch fermentation of Bacillus licheniformis ATCC 9945a in laboratory bioreactor at 37 degrees C. The enzyme was purified by gel filtration chromatographies with 6-fold increase of specific activity and 38% recovery and showed a molecular mass of 31 kDa by SDS-PAGE. The purified enzyme had an optimum pH of 6.5 and optimum temperature of 90 degrees C. The purified alpha-amylase in the presence of CaCl(2) retained 55% of its activity after 6 h of incubation at 70 degrees C. Co(2+), Ni(2+) and Ca(2+) slightly stimulated, while Hg(2+) completely inhibited alpha-amylase activity. Hydrolysis rates of raw triticale, wheat, potato, horseradish and corn starches, at 1% concentration were 63, 60, 59, 52 and 37%, respectively, in a period of 4 h. The properties of the purified enzyme proved its high efficacy for digesting diverse raw starches below gelatinization temperature and, hence, its potential commercial value to use as an industrial enzyme. (C) 2010 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Biochemical Engineering Journal",
title = "Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a",
volume = "53",
number = "2",
pages = "203-209",
doi = "10.1016/j.bej.2010.10.014"
}

Božić, N., Ruiz, J., Lopez-Santin, J.,& Vujčić, Z.. (2011). Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a. in Biochemical Engineering Journal
Elsevier Science Sa, Lausanne., 53(2), 203-209.
https://doi.org/10.1016/j.bej.2010.10.014

Božić N, Ruiz J, Lopez-Santin J, Vujčić Z. Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a. in Biochemical Engineering Journal. 2011;53(2):203-209.
doi:10.1016/j.bej.2010.10.014 .

Božić, Nataša, Ruiz, Jordi, Lopez-Santin, Josep, Vujčić, Zoran, "Production and properties of the highly efficient raw starch digesting alpha-amylase from a Bacillus licheniformis ATCC 9945a" in Biochemical Engineering Journal, 53, no. 2 (2011):203-209,
https://doi.org/10.1016/j.bej.2010.10.014 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Miloradovic, Zoran
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1147
AB  - Yeast cell wall invertase (CWI) was immobilised within 10% gelatin hydrogel. The result of entrapment was the complete immobilisation of all the added CWI. The activity of immobilised biocatalyst was 93 +/- 3 U/g, with activity yield of 30%. The optimum pH was in range of 4.5-5.0 for free and immobilised biocatalyst. The optimum temperature was 60 degrees C for both free and gelatin immobilised CWI. Immobilised CWI was more stable than free CWI above optimum activity temperatures. The K-m of free and immobilised CWI was 35.10 +/- 2.99 mM and 71.45 +/- 3.23 mM, respectively. The V-max, values were estimated as 8.23 +/- 0.24 mM/min and 0.121 +/- 0.002 mM/min, respectively. Immobilised CWI was tested in a batch reactor using 50% sucrose (w/v). After 70 consecutive cycles gelatin immobilised CWI retained 75% of its original activity. (C) 2010 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Cell wall invertase immobilisation within gelatin gel
VL  - 126
IS  - 1
SP  - 236
EP  - 240
DO  - 10.1016/j.foodchem.2010.11.010
ER  - 

@article{
author = "Vujčić, Zoran and Miloradovic, Zoran and Milovanovic, Aleksandra and Božić, Nataša",
year = "2011",
abstract = "Yeast cell wall invertase (CWI) was immobilised within 10% gelatin hydrogel. The result of entrapment was the complete immobilisation of all the added CWI. The activity of immobilised biocatalyst was 93 +/- 3 U/g, with activity yield of 30%. The optimum pH was in range of 4.5-5.0 for free and immobilised biocatalyst. The optimum temperature was 60 degrees C for both free and gelatin immobilised CWI. Immobilised CWI was more stable than free CWI above optimum activity temperatures. The K-m of free and immobilised CWI was 35.10 +/- 2.99 mM and 71.45 +/- 3.23 mM, respectively. The V-max, values were estimated as 8.23 +/- 0.24 mM/min and 0.121 +/- 0.002 mM/min, respectively. Immobilised CWI was tested in a batch reactor using 50% sucrose (w/v). After 70 consecutive cycles gelatin immobilised CWI retained 75% of its original activity. (C) 2010 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Cell wall invertase immobilisation within gelatin gel",
volume = "126",
number = "1",
pages = "236-240",
doi = "10.1016/j.foodchem.2010.11.010"
}

Vujčić, Z., Miloradovic, Z., Milovanovic, A.,& Božić, N.. (2011). Cell wall invertase immobilisation within gelatin gel. in Food Chemistry
Elsevier Sci Ltd, Oxford., 126(1), 236-240.
https://doi.org/10.1016/j.foodchem.2010.11.010

Vujčić Z, Miloradovic Z, Milovanovic A, Božić N. Cell wall invertase immobilisation within gelatin gel. in Food Chemistry. 2011;126(1):236-240.
doi:10.1016/j.foodchem.2010.11.010 .

Vujčić, Zoran, Miloradovic, Zoran, Milovanovic, Aleksandra, Božić, Nataša, "Cell wall invertase immobilisation within gelatin gel" in Food Chemistry, 126, no. 1 (2011):236-240,
https://doi.org/10.1016/j.foodchem.2010.11.010 . .

TY  - JOUR
AU  - Kaluđerović, Goran N.
AU  - Eshkourfu, Rabia O. Mohamad
AU  - Gomez-Ruiz, Santiago
AU  - Mitić, Dragana
AU  - Anđelković, Katarina K.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1069
AB  - The title salt, C(16)H(18)N(6)O(2)(2+)center dot 2ClO(4)(-)center dot 2H(2)O, was obtained unintentionally as a major product in the reaction of Zn(ClO(4))(2)center dot 6H(2)O with the N',N'(2)-bis[(1E)-1-(2-pyridyl)ethylidene]ethanedihydrazide (H(2)L) ligand. The (H(4)L)(2+) cation lies across a centre of inversion. The pyridiniumimine fragments of (H(4)L)(2+) adopt syn orientations. Intramolecular N-H center dot center dot center dot N and N-H center dot center dot center dot O hydrogen bonds lead to the formation of S(5) motifs. In the crystal, neighbouring cations are connected by pi-pi interactions between pyridinium units with a centroid-centroid distance of 3.600 (1) angstrom. Moreover, the crystal components are assembled into two-dimensional layers via N-H center dot center dot center dot O and O-H center dot center dot center dot O hydrogen bonds, with no direct hydrogen-bonding interactions between cations.
PB  - Wiley-Blackwell, Malden
T2  - Acta Crystallographica. Section E: Structure Reports Online
T1  - 2,2 '-{1,1 '-[2,2 '-Oxalylbis(hydrazin-2-yl-1-ylidene)]diethylidyne}dipyridinium bis(perchlorate) dihydrate
VL  - 66
DO  - 10.1107/S1600536810010238
ER  - 

@article{
author = "Kaluđerović, Goran N. and Eshkourfu, Rabia O. Mohamad and Gomez-Ruiz, Santiago and Mitić, Dragana and Anđelković, Katarina K.",
year = "2010",
abstract = "The title salt, C(16)H(18)N(6)O(2)(2+)center dot 2ClO(4)(-)center dot 2H(2)O, was obtained unintentionally as a major product in the reaction of Zn(ClO(4))(2)center dot 6H(2)O with the N',N'(2)-bis[(1E)-1-(2-pyridyl)ethylidene]ethanedihydrazide (H(2)L) ligand. The (H(4)L)(2+) cation lies across a centre of inversion. The pyridiniumimine fragments of (H(4)L)(2+) adopt syn orientations. Intramolecular N-H center dot center dot center dot N and N-H center dot center dot center dot O hydrogen bonds lead to the formation of S(5) motifs. In the crystal, neighbouring cations are connected by pi-pi interactions between pyridinium units with a centroid-centroid distance of 3.600 (1) angstrom. Moreover, the crystal components are assembled into two-dimensional layers via N-H center dot center dot center dot O and O-H center dot center dot center dot O hydrogen bonds, with no direct hydrogen-bonding interactions between cations.",
publisher = "Wiley-Blackwell, Malden",
journal = "Acta Crystallographica. Section E: Structure Reports Online",
title = "2,2 '-{1,1 '-[2,2 '-Oxalylbis(hydrazin-2-yl-1-ylidene)]diethylidyne}dipyridinium bis(perchlorate) dihydrate",
volume = "66",
doi = "10.1107/S1600536810010238"
}

Kaluđerović, G. N., Eshkourfu, R. O. M., Gomez-Ruiz, S., Mitić, D.,& Anđelković, K. K.. (2010). 2,2 '-{1,1 '-[2,2 '-Oxalylbis(hydrazin-2-yl-1-ylidene)]diethylidyne}dipyridinium bis(perchlorate) dihydrate. in Acta Crystallographica. Section E: Structure Reports Online
Wiley-Blackwell, Malden., 66.
https://doi.org/10.1107/S1600536810010238

Kaluđerović GN, Eshkourfu ROM, Gomez-Ruiz S, Mitić D, Anđelković KK. 2,2 '-{1,1 '-[2,2 '-Oxalylbis(hydrazin-2-yl-1-ylidene)]diethylidyne}dipyridinium bis(perchlorate) dihydrate. in Acta Crystallographica. Section E: Structure Reports Online. 2010;66.
doi:10.1107/S1600536810010238 .

Kaluđerović, Goran N., Eshkourfu, Rabia O. Mohamad, Gomez-Ruiz, Santiago, Mitić, Dragana, Anđelković, Katarina K., "2,2 '-{1,1 '-[2,2 '-Oxalylbis(hydrazin-2-yl-1-ylidene)]diethylidyne}dipyridinium bis(perchlorate) dihydrate" in Acta Crystallographica. Section E: Structure Reports Online, 66 (2010),
https://doi.org/10.1107/S1600536810010238 . .

TY  - JOUR
AU  - Miodragović Đenana U.
AU  - Jovanović, Dragoljub
AU  - Bogdanović, Goran A.
AU  - Mitić, Dragana
AU  - Anđelković, Katarina K.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1127
AB  - In the reaction of ZnCl(2) with tacrine hydrochloride in water novel tetracoordinated (C(13)H(15)N(2))(2)[ZnCl(4)]-H(2)O complex was obtained and characterized by elemental analysis, molar conductivity and X-ray analysis. The complex crystallizes in the space group P-1 of the triclinic crystal system. The structure contains two crystallographically different molecules of protonated tacrine present as counter cations, the [ZnCl(4)](2-) complex anion and one water solvent molecule. The counter cations slightly differ in the puckering of the cyclohexene ring. The molecules of protonated tacrine are involved in different intermolecular hydrogen bonds. In the crystal, the hydrogen bonding generates a 3D assembly. In the crystal, pi center dot center dot center dot pi stacking interactions between the rings of protonated tacrine were evidenced. The [ZnCl(4)](2-) complex anion has a distorted tetrahedral geometry. Three out of the four Cl atoms are involved in intermolecular hydrogen bonding. The intermolecular H-bond interactions involving the Cl atoms affect the Zn-CI bond lengths.
AB  - U reakciji ZnCl2 sa takrin-hidrohloridom u vodi, dobijen je novi tetrakoordinovani (C13H15N2)2[ZnCl4]?H2O kompleks koji je okarakterisan pomoću elementalne analize, molarne provodljivosti i rendgenske strukturne analize. Kompleks kristališe u prostornoj grupi P?1 trikliničnog kristalnog sistema. Struktura sadrži dva kristalografski različita molekula protonovanog takrina koji su prisutni kao kontra-katjoni, [ZnCl4]2 kompleksni anjon i molekul kristalne vode. Molekuli katjona se neznatno razlikuju u stepenu nabiranja cikloheksenovog prstena. Molekuli protonovanog takrina su uključeni u različite intermolekulske vodonične veze. Intermolekulsko vodonično vezivanje u kristalu generiše 3D molekulski skup pi...pi interakcije između prstenova protonovanog takrina su primećene u kristalu. [ZnCl4]2- ima distorgovanu tetraedarsku geometriju. Tri od četiri Cl atoma su uključena u intermolekulske vodonične veze. Intermolekulske vodonične interakcije koje uključuju Cl atome utiču na dužinu Zn-Cl veza.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Synthesis and crystal structure of 1,2,3,4-tetrahydro-9-aminoacridine tetrachlorozincate(II) monohydrate
T1  - Sinteza i kristalna struktura 1,2,3,4-tetrahidro-9-aminoakridin-tetrahlorocinkata(II) monohidrata
VL  - 75
IS  - 9
SP  - 1209
EP  - 1218
DO  - 10.2298/JSC100302059M
ER  - 

@article{
author = "Miodragović Đenana U. and Jovanović, Dragoljub and Bogdanović, Goran A. and Mitić, Dragana and Anđelković, Katarina K.",
year = "2010",
abstract = "In the reaction of ZnCl(2) with tacrine hydrochloride in water novel tetracoordinated (C(13)H(15)N(2))(2)[ZnCl(4)]-H(2)O complex was obtained and characterized by elemental analysis, molar conductivity and X-ray analysis. The complex crystallizes in the space group P-1 of the triclinic crystal system. The structure contains two crystallographically different molecules of protonated tacrine present as counter cations, the [ZnCl(4)](2-) complex anion and one water solvent molecule. The counter cations slightly differ in the puckering of the cyclohexene ring. The molecules of protonated tacrine are involved in different intermolecular hydrogen bonds. In the crystal, the hydrogen bonding generates a 3D assembly. In the crystal, pi center dot center dot center dot pi stacking interactions between the rings of protonated tacrine were evidenced. The [ZnCl(4)](2-) complex anion has a distorted tetrahedral geometry. Three out of the four Cl atoms are involved in intermolecular hydrogen bonding. The intermolecular H-bond interactions involving the Cl atoms affect the Zn-CI bond lengths., U reakciji ZnCl2 sa takrin-hidrohloridom u vodi, dobijen je novi tetrakoordinovani (C13H15N2)2[ZnCl4]?H2O kompleks koji je okarakterisan pomoću elementalne analize, molarne provodljivosti i rendgenske strukturne analize. Kompleks kristališe u prostornoj grupi P?1 trikliničnog kristalnog sistema. Struktura sadrži dva kristalografski različita molekula protonovanog takrina koji su prisutni kao kontra-katjoni, [ZnCl4]2 kompleksni anjon i molekul kristalne vode. Molekuli katjona se neznatno razlikuju u stepenu nabiranja cikloheksenovog prstena. Molekuli protonovanog takrina su uključeni u različite intermolekulske vodonične veze. Intermolekulsko vodonično vezivanje u kristalu generiše 3D molekulski skup pi...pi interakcije između prstenova protonovanog takrina su primećene u kristalu. [ZnCl4]2- ima distorgovanu tetraedarsku geometriju. Tri od četiri Cl atoma su uključena u intermolekulske vodonične veze. Intermolekulske vodonične interakcije koje uključuju Cl atome utiču na dužinu Zn-Cl veza.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Synthesis and crystal structure of 1,2,3,4-tetrahydro-9-aminoacridine tetrachlorozincate(II) monohydrate, Sinteza i kristalna struktura 1,2,3,4-tetrahidro-9-aminoakridin-tetrahlorocinkata(II) monohidrata",
volume = "75",
number = "9",
pages = "1209-1218",
doi = "10.2298/JSC100302059M"
}

Miodragović Đenana U., Jovanović, D., Bogdanović, G. A., Mitić, D.,& Anđelković, K. K.. (2010). Synthesis and crystal structure of 1,2,3,4-tetrahydro-9-aminoacridine tetrachlorozincate(II) monohydrate. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 75(9), 1209-1218.
https://doi.org/10.2298/JSC100302059M

Miodragović Đenana U., Jovanović D, Bogdanović GA, Mitić D, Anđelković KK. Synthesis and crystal structure of 1,2,3,4-tetrahydro-9-aminoacridine tetrachlorozincate(II) monohydrate. in Journal of the Serbian Chemical Society. 2010;75(9):1209-1218.
doi:10.2298/JSC100302059M .

Miodragović Đenana U., Jovanović, Dragoljub, Bogdanović, Goran A., Mitić, Dragana, Anđelković, Katarina K., "Synthesis and crystal structure of 1,2,3,4-tetrahydro-9-aminoacridine tetrachlorozincate(II) monohydrate" in Journal of the Serbian Chemical Society, 75, no. 9 (2010):1209-1218,
https://doi.org/10.2298/JSC100302059M . .

TY  - JOUR
AU  - Bjelogrlić, Snežana K.
AU  - Todorović, Tamara
AU  - Bacchi, Alessia
AU  - Zec, Manja
AU  - Sladić, Dušan
AU  - Srdić-Rajić, Tatjana
AU  - Radanović, Dušanka D.
AU  - Radulović, Siniša
AU  - Pelizzi, Giancarlo
AU  - Anđelković, Katarina K.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1081
AB  - Two novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide were synthesized. The structure of Cd(II) complex was determined by X-ray crystallography. The ligand is coordinated in a neutral form via pyridine and azomethine nitrogen atoms and the selenium donor. The cadmium ion completes its five-coordination by two chloride ligands, forming a square-pyramidal geometry. The structure of Zn(II) complex was established by analysis of spectroscopic data, which indicated coordination of the ligand as a bidentate via the selenium and the azomethine nitrogen atoms. The cytotoxic activity of the newly synthesized complexes, as well as if five structurally related complexes and the ligand evaluated against eight tumor cell lines. The new Cd(II) complex showed the highest activity similar to cisplatin with IC50 less than 10 mu M for all cell lines. Cell cycle distribution and apoptosis study showed that Cd(II) complex and cisplatin might have some similarity in anticancer activity, which was not the case for cisplatin and other studied complexes. Effects of the complexes on matrix metalloproteinases (MMPs) MMP-9 and MMP-2 was also studied. Cd(II) and Zn(II) complexes and cisplatin increased MMP-2 activity in supernatants of tested cells. while Ni(II) complex with the same ligand decreased the activity, implying a possible activity in preventing tumor invasion and metastasis processes. (C) 2010 Elsevier Inc. All rights reserved.
PB  - Elsevier Science Inc, New York
T2  - Journal of Inorganic Biochemistry
T1  - Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide Antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes
VL  - 104
IS  - 6
SP  - 673
EP  - 682
DO  - 10.1016/j.jinorgbio.2010.02.009
ER  - 

@article{
author = "Bjelogrlić, Snežana K. and Todorović, Tamara and Bacchi, Alessia and Zec, Manja and Sladić, Dušan and Srdić-Rajić, Tatjana and Radanović, Dušanka D. and Radulović, Siniša and Pelizzi, Giancarlo and Anđelković, Katarina K.",
year = "2010",
abstract = "Two novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide were synthesized. The structure of Cd(II) complex was determined by X-ray crystallography. The ligand is coordinated in a neutral form via pyridine and azomethine nitrogen atoms and the selenium donor. The cadmium ion completes its five-coordination by two chloride ligands, forming a square-pyramidal geometry. The structure of Zn(II) complex was established by analysis of spectroscopic data, which indicated coordination of the ligand as a bidentate via the selenium and the azomethine nitrogen atoms. The cytotoxic activity of the newly synthesized complexes, as well as if five structurally related complexes and the ligand evaluated against eight tumor cell lines. The new Cd(II) complex showed the highest activity similar to cisplatin with IC50 less than 10 mu M for all cell lines. Cell cycle distribution and apoptosis study showed that Cd(II) complex and cisplatin might have some similarity in anticancer activity, which was not the case for cisplatin and other studied complexes. Effects of the complexes on matrix metalloproteinases (MMPs) MMP-9 and MMP-2 was also studied. Cd(II) and Zn(II) complexes and cisplatin increased MMP-2 activity in supernatants of tested cells. while Ni(II) complex with the same ligand decreased the activity, implying a possible activity in preventing tumor invasion and metastasis processes. (C) 2010 Elsevier Inc. All rights reserved.",
publisher = "Elsevier Science Inc, New York",
journal = "Journal of Inorganic Biochemistry",
title = "Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide Antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes",
volume = "104",
number = "6",
pages = "673-682",
doi = "10.1016/j.jinorgbio.2010.02.009"
}

Bjelogrlić, S. K., Todorović, T., Bacchi, A., Zec, M., Sladić, D., Srdić-Rajić, T., Radanović, D. D., Radulović, S., Pelizzi, G.,& Anđelković, K. K.. (2010). Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide Antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes. in Journal of Inorganic Biochemistry
Elsevier Science Inc, New York., 104(6), 673-682.
https://doi.org/10.1016/j.jinorgbio.2010.02.009

Bjelogrlić SK, Todorović T, Bacchi A, Zec M, Sladić D, Srdić-Rajić T, Radanović DD, Radulović S, Pelizzi G, Anđelković KK. Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide Antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes. in Journal of Inorganic Biochemistry. 2010;104(6):673-682.
doi:10.1016/j.jinorgbio.2010.02.009 .

Bjelogrlić, Snežana K., Todorović, Tamara, Bacchi, Alessia, Zec, Manja, Sladić, Dušan, Srdić-Rajić, Tatjana, Radanović, Dušanka D., Radulović, Siniša, Pelizzi, Giancarlo, Anđelković, Katarina K., "Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide Antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes" in Journal of Inorganic Biochemistry, 104, no. 6 (2010):673-682,
https://doi.org/10.1016/j.jinorgbio.2010.02.009 . .

TY  - JOUR
AU  - Božić, Tatjana T.
AU  - Novaković, Irena T.
AU  - Gasic, Miroslav J.
AU  - Juranić, Zorica D.
AU  - Stanojković, Tatjana
AU  - Tufegdžić, Srđan
AU  - Kljajić, Zoran
AU  - Sladić, Dušan
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1057
AB  - Nine alkyl(aryl)thio derivatives of the marine sesquiterpene quinone avarone were synthesized by nucleophilic addition of thiols or thiophenol to avarone. In most cases only one regioisomer was obtained. Their cytotoxic activities, brine shrimp lethality and antibacterial activity were evaluated, as well as those of some previously synthesized avarone derivatives. Anti-HIV activity of two derivatives was tested. Electrochemical properties were determined for all the derivatives in Order to obtain more accurate information on structure-activity relationships. Most derivatives showed cytotoxic activity against tumor cell lines, with IC(50) values less than 10 mu M for some of them, in particular those with electron-donating substituents. The most active Compound was 4'-(methylamino)avarone, with IC(50) value of 2.4 mu M to melanoma Fem-X cells, and no cytotoxicity to normal lymphocytes. (C) 2009 Elsevier Masson SAS. All Fights reserved.
PB  - Elsevier France-Editions Scientifiques Medicales Elsevier, Paris
T2  - European Journal of Medicinal Chemistry
T1  - Synthesis and biological activity of derivatives of the marine quinone avarone
VL  - 45
IS  - 3
SP  - 923
EP  - 929
DO  - 10.1016/j.ejmech.2009.11.033
ER  - 

@article{
author = "Božić, Tatjana T. and Novaković, Irena T. and Gasic, Miroslav J. and Juranić, Zorica D. and Stanojković, Tatjana and Tufegdžić, Srđan and Kljajić, Zoran and Sladić, Dušan",
year = "2010",
abstract = "Nine alkyl(aryl)thio derivatives of the marine sesquiterpene quinone avarone were synthesized by nucleophilic addition of thiols or thiophenol to avarone. In most cases only one regioisomer was obtained. Their cytotoxic activities, brine shrimp lethality and antibacterial activity were evaluated, as well as those of some previously synthesized avarone derivatives. Anti-HIV activity of two derivatives was tested. Electrochemical properties were determined for all the derivatives in Order to obtain more accurate information on structure-activity relationships. Most derivatives showed cytotoxic activity against tumor cell lines, with IC(50) values less than 10 mu M for some of them, in particular those with electron-donating substituents. The most active Compound was 4'-(methylamino)avarone, with IC(50) value of 2.4 mu M to melanoma Fem-X cells, and no cytotoxicity to normal lymphocytes. (C) 2009 Elsevier Masson SAS. All Fights reserved.",
publisher = "Elsevier France-Editions Scientifiques Medicales Elsevier, Paris",
journal = "European Journal of Medicinal Chemistry",
title = "Synthesis and biological activity of derivatives of the marine quinone avarone",
volume = "45",
number = "3",
pages = "923-929",
doi = "10.1016/j.ejmech.2009.11.033"
}

Božić, T. T., Novaković, I. T., Gasic, M. J., Juranić, Z. D., Stanojković, T., Tufegdžić, S., Kljajić, Z.,& Sladić, D.. (2010). Synthesis and biological activity of derivatives of the marine quinone avarone. in European Journal of Medicinal Chemistry
Elsevier France-Editions Scientifiques Medicales Elsevier, Paris., 45(3), 923-929.
https://doi.org/10.1016/j.ejmech.2009.11.033

Božić TT, Novaković IT, Gasic MJ, Juranić ZD, Stanojković T, Tufegdžić S, Kljajić Z, Sladić D. Synthesis and biological activity of derivatives of the marine quinone avarone. in European Journal of Medicinal Chemistry. 2010;45(3):923-929.
doi:10.1016/j.ejmech.2009.11.033 .

Božić, Tatjana T., Novaković, Irena T., Gasic, Miroslav J., Juranić, Zorica D., Stanojković, Tatjana, Tufegdžić, Srđan, Kljajić, Zoran, Sladić, Dušan, "Synthesis and biological activity of derivatives of the marine quinone avarone" in European Journal of Medicinal Chemistry, 45, no. 3 (2010):923-929,
https://doi.org/10.1016/j.ejmech.2009.11.033 . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Lončar, Nikola L.
AU  - Dojnov, Biljana
AU  - Milovanovic, Aleksandra
AU  - Vujčić, Miroslava
AU  - Božić, Nataša
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1060
AB  - Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber
VL  - 121
IS  - 2
SP  - 418
EP  - 423
DO  - 10.1016/j.foodchem.2009.12.058
ER  - 

@article{
author = "Vujčić, Zoran and Lončar, Nikola L. and Dojnov, Biljana and Milovanovic, Aleksandra and Vujčić, Miroslava and Božić, Nataša",
year = "2010",
abstract = "Potato juice (a waste product from the starch industry) is a potential source of novel enzymes for food applications. For use in the production and improvement of food protein hydrolysates, commercially available exopeptidases, predominantly aminopeptidases, are recommended. The present study was performed to explore possible biotechnological interest of leucyl aminopeptidase (LAP) activity in the potato tuber. The LAP from potato tuber was purified and characterised. Specific LAP activity was increased 200-fold by purification of the crude extract. The purified enzyme had a pH optimum of 9.0 and temperature optimum of 45 degrees C. LAP hydrolysed leucine-, alanine- and lysine-p-nitroanilide to a similar degree. The most efficient inhibitor was 1,10-phenanthroline. Almost all divalent cations tested inhibited the enzyme activity, while Co2+ stimulated LAP activity by over 100%. The purified LAP had a molecular weight of 90 kDa with an isoelectric point of 5.45. Sodium dodecylsulfate-polyacrylamide gel electrophoresis revealed one band of 48 kDa. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber",
volume = "121",
number = "2",
pages = "418-423",
doi = "10.1016/j.foodchem.2009.12.058"
}

Vujčić, Z., Lončar, N. L., Dojnov, B., Milovanovic, A., Vujčić, M.,& Božić, N.. (2010). Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. in Food Chemistry
Elsevier Sci Ltd, Oxford., 121(2), 418-423.
https://doi.org/10.1016/j.foodchem.2009.12.058

Vujčić Z, Lončar NL, Dojnov B, Milovanovic A, Vujčić M, Božić N. Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber. in Food Chemistry. 2010;121(2):418-423.
doi:10.1016/j.foodchem.2009.12.058 .

Vujčić, Zoran, Lončar, Nikola L., Dojnov, Biljana, Milovanovic, Aleksandra, Vujčić, Miroslava, Božić, Nataša, "Characterisation of leucyl aminopeptidase from Solanum tuberosum tuber" in Food Chemistry, 121, no. 2 (2010):418-423,
https://doi.org/10.1016/j.foodchem.2009.12.058 . .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Vujčić, Zoran
AU  - Božić, Nataša
AU  - Ivanovic, Jelisaveta
AU  - Nenadovic, Vera
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1107
AB  - Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 9.0 (optimum pH range 8.5-9.5) and temperature optimum of 45 degrees C with the KM ratio of 0.065 mM for benzoyl-arginine-p-nitroanilide (BApNA). Among a number of inhibitors tested, the most efficient was benzamidine (K-I value of 0.012 mM, Ic(50) value of 0.204 mM) while inhibition of TLE activity by SBTI, TLCK, and PMSF was partial. Almost all divalent cations tested enhanced the enzyme activity, amongst them Co2+ and Mn2+ stimulated TLE activity for 2.5 times. The purified TLE (after gel-filtration on Superose 12 column) had a molecular mass of 37.5 kDa with an isoelectric point over 9.3. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 38 kDa, suggesting that the enzyme is a monomer. (C) 2010 Wiley Periodicals, Inc.
PB  - Wiley-Blackwell, Hoboken
T2  - Archives of Insect Biochemistry and Physiology
T1  - Purification and Properties of Trypsin-Like Enzyme from  the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae
VL  - 74
IS  - 4
SP  - 232
EP  - 246
DO  - 10.1002/arch.20371
ER  - 

@article{
author = "Lončar, Nikola L. and Vujčić, Zoran and Božić, Nataša and Ivanovic, Jelisaveta and Nenadovic, Vera",
year = "2010",
abstract = "Trypsin-like enzyme (TLE) from the anterior midgut of Morimus funereus larvae was purified by anion exchange chromatography and gel filtration chromatography and characterized. Specific TLE activity was increased 322-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 9.0 (optimum pH range 8.5-9.5) and temperature optimum of 45 degrees C with the KM ratio of 0.065 mM for benzoyl-arginine-p-nitroanilide (BApNA). Among a number of inhibitors tested, the most efficient was benzamidine (K-I value of 0.012 mM, Ic(50) value of 0.204 mM) while inhibition of TLE activity by SBTI, TLCK, and PMSF was partial. Almost all divalent cations tested enhanced the enzyme activity, amongst them Co2+ and Mn2+ stimulated TLE activity for 2.5 times. The purified TLE (after gel-filtration on Superose 12 column) had a molecular mass of 37.5 kDa with an isoelectric point over 9.3. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 38 kDa, suggesting that the enzyme is a monomer. (C) 2010 Wiley Periodicals, Inc.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Archives of Insect Biochemistry and Physiology",
title = "Purification and Properties of Trypsin-Like Enzyme from  the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae",
volume = "74",
number = "4",
pages = "232-246",
doi = "10.1002/arch.20371"
}

Lončar, N. L., Vujčić, Z., Božić, N., Ivanovic, J.,& Nenadovic, V.. (2010). Purification and Properties of Trypsin-Like Enzyme from  the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae. in Archives of Insect Biochemistry and Physiology
Wiley-Blackwell, Hoboken., 74(4), 232-246.
https://doi.org/10.1002/arch.20371

Lončar NL, Vujčić Z, Božić N, Ivanovic J, Nenadovic V. Purification and Properties of Trypsin-Like Enzyme from  the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae. in Archives of Insect Biochemistry and Physiology. 2010;74(4):232-246.
doi:10.1002/arch.20371 .

Lončar, Nikola L., Vujčić, Zoran, Božić, Nataša, Ivanovic, Jelisaveta, Nenadovic, Vera, "Purification and Properties of Trypsin-Like Enzyme from  the Midgut of Morimus Funereus (Coleoptera, Cerambycidae) Larvae" in Archives of Insect Biochemistry and Physiology, 74, no. 4 (2010):232-246,
https://doi.org/10.1002/arch.20371 . .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1109
AB  - alpha-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI  lt  3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa.
AB  - Upoređene su izoforme α-amilaze larvi Cerambyx cerdo sakupljenih iz prirode (ML i SL) i gajenih na veštačkoj podlozi u laboratoriji (ADL). Zimogramskom detekcijom posle IEF-a po tri izoforme su detektovane u ML i SL ekstraktima, a u ADL dve izoforme. Sve amilazne izoforme iz C. cerdo su bile kisele (pI  lt  3.5). Zimogramskom detekcijom posle nativne elektroforeze sedam izoformi je detektovano u ML ekstraktu, šest u SL ekstraktu i četiri u ADL ekstraktu. Najveća amilazna aktivnost je detektovana u ADL ekstraktu. Svi ekstrakti srednjih creva larvi C. cerdo su frakcionisani na koloni Superose 12 HR. Molekulska masa ACC-a je bila 34 kDa.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Comparison of Alpha-Amylase Isoforms from  the Midgut of Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae Developed in the Wild and on An Artificial Diet
T1  - Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi
VL  - 62
IS  - 3
SP  - 575
EP  - 584
DO  - 10.2298/ABS1003575D
ER  - 

@article{
author = "Dojnov, Biljana and Lončar, Nikola L. and Božić, Nataša and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2010",
abstract = "alpha-Amylase isoforms of Cerambyx cerdo larvae from the wild (ML and SL) and reared in the laboratory (ADL) were compared. Three amylase isoforms were presented in the SL and ML extracts while two isoforms were presented in the ADL according to zymogram after isoelectric focusing (IEF). All C. cerdo amylase isoforms were acidic proteins (pI  lt  3.5). Seven amylase isoforms (ACC 1-7) from the midgut of C. cerdo larvae were found in the ML midgut extract, six in the SL extract, and four in the ADL extract according to native PAGE zymogram. The ADL amylase had the highest activity. All crude midgut extracts of C. cerdo larvae were fractionated on a Superose 12 HR column. The molecular mass of the ACC was estimated to be 34 kDa., Upoređene su izoforme α-amilaze larvi Cerambyx cerdo sakupljenih iz prirode (ML i SL) i gajenih na veštačkoj podlozi u laboratoriji (ADL). Zimogramskom detekcijom posle IEF-a po tri izoforme su detektovane u ML i SL ekstraktima, a u ADL dve izoforme. Sve amilazne izoforme iz C. cerdo su bile kisele (pI  lt  3.5). Zimogramskom detekcijom posle nativne elektroforeze sedam izoformi je detektovano u ML ekstraktu, šest u SL ekstraktu i četiri u ADL ekstraktu. Najveća amilazna aktivnost je detektovana u ADL ekstraktu. Svi ekstrakti srednjih creva larvi C. cerdo su frakcionisani na koloni Superose 12 HR. Molekulska masa ACC-a je bila 34 kDa.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Comparison of Alpha-Amylase Isoforms from  the Midgut of Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae Developed in the Wild and on An Artificial Diet, Uporedna analiza izoformi α-amilaze iz srednjeg creva larvi Cerambyx cerdo L. (Coleoptera: Cerambycidae) iz prirode i gajenih na veštačkoj podlozi",
volume = "62",
number = "3",
pages = "575-584",
doi = "10.2298/ABS1003575D"
}

Dojnov, B., Lončar, N. L., Božić, N., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2010). Comparison of Alpha-Amylase Isoforms from  the Midgut of Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae Developed in the Wild and on An Artificial Diet. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 62(3), 575-584.
https://doi.org/10.2298/ABS1003575D

Dojnov B, Lončar NL, Božić N, Nenadovic V, Ivanovic J, Vujčić Z. Comparison of Alpha-Amylase Isoforms from  the Midgut of Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae Developed in the Wild and on An Artificial Diet. in Archives of biological sciences. 2010;62(3):575-584.
doi:10.2298/ABS1003575D .

Dojnov, Biljana, Lončar, Nikola L., Božić, Nataša, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Comparison of Alpha-Amylase Isoforms from  the Midgut of Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae Developed in the Wild and on An Artificial Diet" in Archives of biological sciences, 62, no. 3 (2010):575-584,
https://doi.org/10.2298/ABS1003575D . .

TY  - JOUR
AU  - Vujčić, Zoran
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Anđelković, Uroš
AU  - Lončar, Nikola L.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1133
AB  - Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.
PB  - Amer Chemical Soc, Washington
T2  - Journal of Agricultural and Food Chemistry
T1  - Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar
VL  - 58
IS  - 22
SP  - 11896
EP  - 11900
DO  - 10.1021/jf101836r
ER  - 

@article{
author = "Vujčić, Zoran and Milovanovic, Aleksandra and Božić, Nataša and Dojnov, Biljana and Vujčić, Miroslava and Anđelković, Uroš and Lončar, Nikola L.",
year = "2010",
abstract = "Yeast cell wall invertase (CWI) was modified with dimethyl suberimidate, glutaraldehyde, formaldehyde, and sodium periodate. Retained activity after modification was 45% for CWI modified with formaldehyde, 77% for CWI modified with sodium periodate, 80% for CWI modified with glutaraldehyde, and 115% for CWI modified with dimethyl suberimidate. Chemically modified and native CWIs showed significantly broad pH stability (pH 3-11), whereas after incubations at 50, 60, and 70 degrees C, CWI modified with glutaraldehyde showed the highest thermostability. Optimum pH for CWI modified with glutaraldehyde was between 4 and 5, whereas optimum temperature was at 60 degrees C. Comparison to CWI modified with glutaraldehyde after immobilization within alginate beads showed broader pH optimum (4.0-5.5) as well as broader temperature optimum (55-70 degrees C). Column bed reactor packed with the immobilized CWI modified with glutaraldehyde was successfully used for the 95% inversion of 60% (w/w) sucrose at the flow rate of 3 bed volumes per hour, pH 4.9, and 45 degrees C. A 1 month productivity of 3844 kg of inverted sugar/kg of the immobilisate was obtained.",
publisher = "Amer Chemical Soc, Washington",
journal = "Journal of Agricultural and Food Chemistry",
title = "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar",
volume = "58",
number = "22",
pages = "11896-11900",
doi = "10.1021/jf101836r"
}

Vujčić, Z., Milovanovic, A., Božić, N., Dojnov, B., Vujčić, M., Anđelković, U.,& Lončar, N. L.. (2010). Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry
Amer Chemical Soc, Washington., 58(22), 11896-11900.
https://doi.org/10.1021/jf101836r

Vujčić Z, Milovanovic A, Božić N, Dojnov B, Vujčić M, Anđelković U, Lončar NL. Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar. in Journal of Agricultural and Food Chemistry. 2010;58(22):11896-11900.
doi:10.1021/jf101836r .

Vujčić, Zoran, Milovanovic, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava, Anđelković, Uroš, Lončar, Nikola L., "Immobilization of Cell Wall Invertase Modified with Glutaraldehyde for Continuous Production of Invert Sugar" in Journal of Agricultural and Food Chemistry, 58, no. 22 (2010):11896-11900,
https://doi.org/10.1021/jf101836r . .

TY  - JOUR
AU  - Anđelković, Uroš
AU  - Picuric, Srdjan
AU  - Vujčić, Zoran
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1052
AB  - Four external invertase isoforms (EINV1, EINV2, EINV3 and EINV4) from Saccharomyces cerevisiae were highly purified by isoelectric precipitation, ethanol precipitation, ion-exchange on QAE-Sephadex and gel filtration using Sephacryl S-200. Unlike previously published procedures for external invertase purification, a specially designed step elution was applied on QAE-Sephadex which enabled the separation of four isoforms. The isoforms have the same molecular mass and catalytic properties: K-m for sucrose (25.6 mM), pH optimum (3.5-5.0) and temperature optimum (60 degrees C), but they exhibit significant difference in pl values, thermal stability and chemical reactivity. Deglycosylation Studies showed that the observed differences between isoforms arise from posttranslational modifications. Results showed that external invertase is a mixture of at least four isoforms, but in order to improve the efficiency of food industry processes, only the most stable isoform (EINV1) should be purified and utilised. Substantially different chemical reactivity of the isoforms could be used to improve the yield of covalent immobilization procedures. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms
VL  - 120
IS  - 3
SP  - 799
EP  - 804
DO  - 10.1016/j.foodchem.2009.11.013
ER  - 

@article{
author = "Anđelković, Uroš and Picuric, Srdjan and Vujčić, Zoran",
year = "2010",
abstract = "Four external invertase isoforms (EINV1, EINV2, EINV3 and EINV4) from Saccharomyces cerevisiae were highly purified by isoelectric precipitation, ethanol precipitation, ion-exchange on QAE-Sephadex and gel filtration using Sephacryl S-200. Unlike previously published procedures for external invertase purification, a specially designed step elution was applied on QAE-Sephadex which enabled the separation of four isoforms. The isoforms have the same molecular mass and catalytic properties: K-m for sucrose (25.6 mM), pH optimum (3.5-5.0) and temperature optimum (60 degrees C), but they exhibit significant difference in pl values, thermal stability and chemical reactivity. Deglycosylation Studies showed that the observed differences between isoforms arise from posttranslational modifications. Results showed that external invertase is a mixture of at least four isoforms, but in order to improve the efficiency of food industry processes, only the most stable isoform (EINV1) should be purified and utilised. Substantially different chemical reactivity of the isoforms could be used to improve the yield of covalent immobilization procedures. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms",
volume = "120",
number = "3",
pages = "799-804",
doi = "10.1016/j.foodchem.2009.11.013"
}

Anđelković, U., Picuric, S.,& Vujčić, Z.. (2010). Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms. in Food Chemistry
Elsevier Sci Ltd, Oxford., 120(3), 799-804.
https://doi.org/10.1016/j.foodchem.2009.11.013

Anđelković U, Picuric S, Vujčić Z. Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms. in Food Chemistry. 2010;120(3):799-804.
doi:10.1016/j.foodchem.2009.11.013 .

Anđelković, Uroš, Picuric, Srdjan, Vujčić, Zoran, "Purification and characterisation of Saccharomyces cerevisiae external invertase isoforms" in Food Chemistry, 120, no. 3 (2010):799-804,
https://doi.org/10.1016/j.foodchem.2009.11.013 . .

TY  - JOUR
AU  - Todorović, Tamara
AU  - Bacchi, Alessia
AU  - Sladić, Dušan
AU  - Todorović, Nina
AU  - Božić, Tatjana T.
AU  - Radanović, Dušanka D.
AU  - Filipović, Nenad R.
AU  - Pelizzi, Giancarlo
AU  - Anđelković, Katarina K.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/873
AB  - Five new complexes of Pt(II), Pd(II), Co(III) and Ni(II) with 2-pyridine(quinoline) carboxaldehyde selenose-micarbazones were synthesized and characterized. Crystal structures of Pt(II) complex with the pyridine derivative and Co(III) complex with the quinoline derivative were determined. In all complexes the ligands were coordinated through N(2)Se donor atom set forming either square-planar (Pt, Pd) or octahedral (Co, Ni) geometry. All complexes showed biological activity. (C) 2009 Elsevier B. V. All rights reserved.
PB  - Elsevier Science Sa, Lausanne
T2  - Inorganica Chimica Acta
T1  - Synthesis, characterization and biological activity evaluation of Pt(II), Pd(II), Co(III) and Ni(II) complexes with N-heteroaromatic selenosemicarbazones
VL  - 362
IS  - 10
SP  - 3813
EP  - 3820
DO  - 10.1016/j.ica.2009.04.047
ER  - 

@article{
author = "Todorović, Tamara and Bacchi, Alessia and Sladić, Dušan and Todorović, Nina and Božić, Tatjana T. and Radanović, Dušanka D. and Filipović, Nenad R. and Pelizzi, Giancarlo and Anđelković, Katarina K.",
year = "2009",
abstract = "Five new complexes of Pt(II), Pd(II), Co(III) and Ni(II) with 2-pyridine(quinoline) carboxaldehyde selenose-micarbazones were synthesized and characterized. Crystal structures of Pt(II) complex with the pyridine derivative and Co(III) complex with the quinoline derivative were determined. In all complexes the ligands were coordinated through N(2)Se donor atom set forming either square-planar (Pt, Pd) or octahedral (Co, Ni) geometry. All complexes showed biological activity. (C) 2009 Elsevier B. V. All rights reserved.",
publisher = "Elsevier Science Sa, Lausanne",
journal = "Inorganica Chimica Acta",
title = "Synthesis, characterization and biological activity evaluation of Pt(II), Pd(II), Co(III) and Ni(II) complexes with N-heteroaromatic selenosemicarbazones",
volume = "362",
number = "10",
pages = "3813-3820",
doi = "10.1016/j.ica.2009.04.047"
}

Todorović, T., Bacchi, A., Sladić, D., Todorović, N., Božić, T. T., Radanović, D. D., Filipović, N. R., Pelizzi, G.,& Anđelković, K. K.. (2009). Synthesis, characterization and biological activity evaluation of Pt(II), Pd(II), Co(III) and Ni(II) complexes with N-heteroaromatic selenosemicarbazones. in Inorganica Chimica Acta
Elsevier Science Sa, Lausanne., 362(10), 3813-3820.
https://doi.org/10.1016/j.ica.2009.04.047

Todorović T, Bacchi A, Sladić D, Todorović N, Božić TT, Radanović DD, Filipović NR, Pelizzi G, Anđelković KK. Synthesis, characterization and biological activity evaluation of Pt(II), Pd(II), Co(III) and Ni(II) complexes with N-heteroaromatic selenosemicarbazones. in Inorganica Chimica Acta. 2009;362(10):3813-3820.
doi:10.1016/j.ica.2009.04.047 .

Todorović, Tamara, Bacchi, Alessia, Sladić, Dušan, Todorović, Nina, Božić, Tatjana T., Radanović, Dušanka D., Filipović, Nenad R., Pelizzi, Giancarlo, Anđelković, Katarina K., "Synthesis, characterization and biological activity evaluation of Pt(II), Pd(II), Co(III) and Ni(II) complexes with N-heteroaromatic selenosemicarbazones" in Inorganica Chimica Acta, 362, no. 10 (2009):3813-3820,
https://doi.org/10.1016/j.ica.2009.04.047 . .

TY  - JOUR
AU  - Todorović, Tamara
AU  - Rychlewska, Urszula
AU  - Warżajtis, Beata
AU  - Radanović, Dušanka D.
AU  - Filipović, Nenad R.
AU  - Pajic, Ivana A.
AU  - Sladić, Dušan
AU  - Anđelković, Katarina K.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1007
AB  - The bimetallic [Ni-2(H(2)L2)(2)](ClO4)(4) (1), [Ni-2(HL2)(H(2)L2)](ClO4)(3) (2) and [Zn-2(H(2)L2)(2)](BF4)(4) (3) complexes (H(2)L2 = N',N'(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide) were synthesized and characterized. The structure of complexes (1) and (2) was established by X-ray analysis. NMR spectroscopy was used for the characterization of complex (3). The complexes (1) and (2) were obtained from the same synthetic reaction and two crystal types of these complexes have been isolated during the fractional crystallization process. In complex (1) each Ni(II) ion is coordinated with two NNO donor atom sets from two H(2)L2 ligands forming an octahedral geometry. Similarly, in complex (2) the octahedral geometry of each Ni(II) ion is attained by coordination of two NNO donor atom sets, one from the neutral and the other from the monoanionic form of the ligand. The antimicrobial activity of the ligand and complexes is also presented. (C) 2009 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Polyhedron
T1  - Synthesis, characterization and antimicrobial activity of Ni(II) and Zn(II) complexes with N ',N '(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide. Crystal structures of two highly solvated bimetallic complexes of Ni(II)
VL  - 28
IS  - 12
SP  - 2397
EP  - 2402
DO  - 10.1016/j.poly.2009.05.002
ER  - 

@article{
author = "Todorović, Tamara and Rychlewska, Urszula and Warżajtis, Beata and Radanović, Dušanka D. and Filipović, Nenad R. and Pajic, Ivana A. and Sladić, Dušan and Anđelković, Katarina K.",
year = "2009",
abstract = "The bimetallic [Ni-2(H(2)L2)(2)](ClO4)(4) (1), [Ni-2(HL2)(H(2)L2)](ClO4)(3) (2) and [Zn-2(H(2)L2)(2)](BF4)(4) (3) complexes (H(2)L2 = N',N'(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide) were synthesized and characterized. The structure of complexes (1) and (2) was established by X-ray analysis. NMR spectroscopy was used for the characterization of complex (3). The complexes (1) and (2) were obtained from the same synthetic reaction and two crystal types of these complexes have been isolated during the fractional crystallization process. In complex (1) each Ni(II) ion is coordinated with two NNO donor atom sets from two H(2)L2 ligands forming an octahedral geometry. Similarly, in complex (2) the octahedral geometry of each Ni(II) ion is attained by coordination of two NNO donor atom sets, one from the neutral and the other from the monoanionic form of the ligand. The antimicrobial activity of the ligand and complexes is also presented. (C) 2009 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Polyhedron",
title = "Synthesis, characterization and antimicrobial activity of Ni(II) and Zn(II) complexes with N ',N '(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide. Crystal structures of two highly solvated bimetallic complexes of Ni(II)",
volume = "28",
number = "12",
pages = "2397-2402",
doi = "10.1016/j.poly.2009.05.002"
}

Todorović, T., Rychlewska, U., Warżajtis, B., Radanović, D. D., Filipović, N. R., Pajic, I. A., Sladić, D.,& Anđelković, K. K.. (2009). Synthesis, characterization and antimicrobial activity of Ni(II) and Zn(II) complexes with N ',N '(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide. Crystal structures of two highly solvated bimetallic complexes of Ni(II). in Polyhedron
Pergamon-Elsevier Science Ltd, Oxford., 28(12), 2397-2402.
https://doi.org/10.1016/j.poly.2009.05.002

Todorović T, Rychlewska U, Warżajtis B, Radanović DD, Filipović NR, Pajic IA, Sladić D, Anđelković KK. Synthesis, characterization and antimicrobial activity of Ni(II) and Zn(II) complexes with N ',N '(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide. Crystal structures of two highly solvated bimetallic complexes of Ni(II). in Polyhedron. 2009;28(12):2397-2402.
doi:10.1016/j.poly.2009.05.002 .

Todorović, Tamara, Rychlewska, Urszula, Warżajtis, Beata, Radanović, Dušanka D., Filipović, Nenad R., Pajic, Ivana A., Sladić, Dušan, Anđelković, Katarina K., "Synthesis, characterization and antimicrobial activity of Ni(II) and Zn(II) complexes with N ',N '(2)-bis[(1E)-1-(2-pyridyl)ethylidene]propanedihydrazide. Crystal structures of two highly solvated bimetallic complexes of Ni(II)" in Polyhedron, 28, no. 12 (2009):2397-2402,
https://doi.org/10.1016/j.poly.2009.05.002 . .

TY  - JOUR
AU  - Radanović, Dušanka D.
AU  - Kaluđerović, Goran N.
AU  - Gomez-Ruiz, Santiago
AU  - Sladić, Dušan
AU  - Šumar-Ristović, Maja
AU  - Brčeski, Ilija
AU  - Anđelković, Katarina K.
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/603
AB  - In an attempt to synthesize a Cr(III) complex of 20-[1-(2-pyridinyl)ethylidene]oxamohydrazide an azine product 2-{1-[(1-(2-pyridinio)ethylidene)hydrazono]ethyl} pyridinium diperchlorate was obtained by an electrophilic acyl substitution catalyzed by Cr(III). Its structure was determined by X-ray crystal analysis and showed significant changes in comparison to the corresponding unprotonated compound. The 2-{1-[(1-(2-pyridinio)ethylidene)hydrazono] ethyl}pyridinium diperchlorate crystallizes in the space group P2(1)/n of the monoclinic crystal system with unit cell parameters a = 14.3809(3) angstrom, b = 24.1516(5) angstrom, c = 15.4471(3) angstrom, beta = 99.930(2)degrees, V = 5284.74(19) angstrom(3) and Z = 12, i.e. three molecules per asymmetric unit.
PB  - Springer/Plenum Publishers, New York
T2  - Journal of Chemical Crystallography
T1  - Crystal Structure of 2-{1-[(1-(2-Pyridinio)ethylidene) hydrazono]ethyl}pyridinium diperchlorate, the Product of Template Condensation in the Presence of Cr(III)
VL  - 39
IS  - 2
SP  - 138
EP  - 142
DO  - 10.1007/s10870-008-9443-6
ER  - 

@article{
author = "Radanović, Dušanka D. and Kaluđerović, Goran N. and Gomez-Ruiz, Santiago and Sladić, Dušan and Šumar-Ristović, Maja and Brčeski, Ilija and Anđelković, Katarina K.",
year = "2009",
abstract = "In an attempt to synthesize a Cr(III) complex of 20-[1-(2-pyridinyl)ethylidene]oxamohydrazide an azine product 2-{1-[(1-(2-pyridinio)ethylidene)hydrazono]ethyl} pyridinium diperchlorate was obtained by an electrophilic acyl substitution catalyzed by Cr(III). Its structure was determined by X-ray crystal analysis and showed significant changes in comparison to the corresponding unprotonated compound. The 2-{1-[(1-(2-pyridinio)ethylidene)hydrazono] ethyl}pyridinium diperchlorate crystallizes in the space group P2(1)/n of the monoclinic crystal system with unit cell parameters a = 14.3809(3) angstrom, b = 24.1516(5) angstrom, c = 15.4471(3) angstrom, beta = 99.930(2)degrees, V = 5284.74(19) angstrom(3) and Z = 12, i.e. three molecules per asymmetric unit.",
publisher = "Springer/Plenum Publishers, New York",
journal = "Journal of Chemical Crystallography",
title = "Crystal Structure of 2-{1-[(1-(2-Pyridinio)ethylidene) hydrazono]ethyl}pyridinium diperchlorate, the Product of Template Condensation in the Presence of Cr(III)",
volume = "39",
number = "2",
pages = "138-142",
doi = "10.1007/s10870-008-9443-6"
}

Radanović, D. D., Kaluđerović, G. N., Gomez-Ruiz, S., Sladić, D., Šumar-Ristović, M., Brčeski, I.,& Anđelković, K. K.. (2009). Crystal Structure of 2-{1-[(1-(2-Pyridinio)ethylidene) hydrazono]ethyl}pyridinium diperchlorate, the Product of Template Condensation in the Presence of Cr(III). in Journal of Chemical Crystallography
Springer/Plenum Publishers, New York., 39(2), 138-142.
https://doi.org/10.1007/s10870-008-9443-6

Radanović DD, Kaluđerović GN, Gomez-Ruiz S, Sladić D, Šumar-Ristović M, Brčeski I, Anđelković KK. Crystal Structure of 2-{1-[(1-(2-Pyridinio)ethylidene) hydrazono]ethyl}pyridinium diperchlorate, the Product of Template Condensation in the Presence of Cr(III). in Journal of Chemical Crystallography. 2009;39(2):138-142.
doi:10.1007/s10870-008-9443-6 .

Radanović, Dušanka D., Kaluđerović, Goran N., Gomez-Ruiz, Santiago, Sladić, Dušan, Šumar-Ristović, Maja, Brčeski, Ilija, Anđelković, Katarina K., "Crystal Structure of 2-{1-[(1-(2-Pyridinio)ethylidene) hydrazono]ethyl}pyridinium diperchlorate, the Product of Template Condensation in the Presence of Cr(III)" in Journal of Chemical Crystallography, 39, no. 2 (2009):138-142,
https://doi.org/10.1007/s10870-008-9443-6 . .

TY  - JOUR
AU  - Lončar, Nikola L.
AU  - Božić, Nataša
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1038
AB  - The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine.
AB  - pH vrednost duž srednjeg creva larvi M. funereus se razlikuje, kisela je u regionu prednjeg dela, dok je u srednjem i zadnjem delu bazna. Elastazama i himotripsinima slična aktivnost je najveća u srednjem delu srednjeg creva dok je u prednjem delu detektovana mala vrednost, a u zadnjem delu zanemarljiva. Tripsinima slična aktivnost je detektovana duž celog srednjeg creva, s tim da se više od 90 % aktivnosti detektuje u prednjem delu srednjeg creva. Zastupljenost elastazama i himotripsinima sličnih endopeptidaza je zanemarljivo mala u poređenju sa zastupljenošću tripsinima sličnih enzima. U prednjem delu srednjeg creva nalaze se dve izoforme tripsinima sličnih enzima, sa baznim pI vrednostima, koje su skoro u potpunosti inhibirane benzamidinom.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Characterization of Trypsin-Like Enzymes from  the Midgut of Morimus Funereus (Coleoptera: Cerambycidae) Larvae
T1  - Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)
VL  - 61
IS  - 4
SP  - 713
EP  - 718
DO  - 10.2298/ABS0904713L
ER  - 

@article{
author = "Lončar, Nikola L. and Božić, Nataša and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2009",
abstract = "The pH along the midgut of M. funereus larvae had different values, being acidic in the anterior section and basic in the middle and posterior sections. Elastase- and chymotrypsin-like activities were highest in the middle, low in the anterior, and negligible in the posterior section of the midgut. Trypsin-like activities were detected along the whole midgut, with more than 90% of activity in the anterior section. The level of elastase- and chymotrypsin-like activity was very low compared to trypsin-like activity. In the anterior section of the midgut, two isoforms of trypsin-like enzymes were found, both being basic and almost completely inhibited by benzamidine., pH vrednost duž srednjeg creva larvi M. funereus se razlikuje, kisela je u regionu prednjeg dela, dok je u srednjem i zadnjem delu bazna. Elastazama i himotripsinima slična aktivnost je najveća u srednjem delu srednjeg creva dok je u prednjem delu detektovana mala vrednost, a u zadnjem delu zanemarljiva. Tripsinima slična aktivnost je detektovana duž celog srednjeg creva, s tim da se više od 90 % aktivnosti detektuje u prednjem delu srednjeg creva. Zastupljenost elastazama i himotripsinima sličnih endopeptidaza je zanemarljivo mala u poređenju sa zastupljenošću tripsinima sličnih enzima. U prednjem delu srednjeg creva nalaze se dve izoforme tripsinima sličnih enzima, sa baznim pI vrednostima, koje su skoro u potpunosti inhibirane benzamidinom.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Characterization of Trypsin-Like Enzymes from  the Midgut of Morimus Funereus (Coleoptera: Cerambycidae) Larvae, Karakterizacija tripsinima-sličnih enzima srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)",
volume = "61",
number = "4",
pages = "713-718",
doi = "10.2298/ABS0904713L"
}

Lončar, N. L., Božić, N., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2009). Characterization of Trypsin-Like Enzymes from  the Midgut of Morimus Funereus (Coleoptera: Cerambycidae) Larvae. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 61(4), 713-718.
https://doi.org/10.2298/ABS0904713L

Lončar NL, Božić N, Nenadovic V, Ivanovic J, Vujčić Z. Characterization of Trypsin-Like Enzymes from  the Midgut of Morimus Funereus (Coleoptera: Cerambycidae) Larvae. in Archives of biological sciences. 2009;61(4):713-718.
doi:10.2298/ABS0904713L .

Lončar, Nikola L., Božić, Nataša, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Characterization of Trypsin-Like Enzymes from  the Midgut of Morimus Funereus (Coleoptera: Cerambycidae) Larvae" in Archives of biological sciences, 61, no. 4 (2009):713-718,
https://doi.org/10.2298/ABS0904713L . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Dojnov, Biljana
AU  - Milovanovic, Aleksandra
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/963
AB  - Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities.
AB  - Primenom specifičnih hromogenih supstrata, klasno-specifičnih inhibitora i zimogramske analize identifikovano je nekoliko klasa peptidaza u sirovom ekstraktu srednjeg creva larvi koleoptere Morimus funereus. Zimogramskom analizom sa želatinom kao supstratom i fenilmetilsulfonil-fluoridom kao inhibitorom utvrđeno je da su serin-peptidaze najzastupljenije peptidaze u ekstraktu srednjeg creva larvi M. funereus. Zimogramskom analizom sa želatinom kao supstratom i 1,10-fenantrolinom kaoinhibitorom takođe su detektovane metalopeptidaze. Analizom serin-peptidaza, upotrebom specifičnih hromogenih supstrata, dokazano je da su dominantni elastazi-slični enzimi u sirovom ekstraktu srednjeg creva larvi M. funereus, dok su himotripsinima- i tripsinima-slični enzimi manje zastupljeni.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae
T1  - Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)
VL  - 60
IS  - 3
SP  - 403
EP  - 409
DO  - 10.2298/ABS0803403B
ER  - 

@article{
author = "Božić, Nataša and Dojnov, Biljana and Milovanovic, Aleksandra and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2008",
abstract = "Application of specific chromogenic substrates, use of class-specific inhibitors, and zymogram analysis enabled us to identify several peptidase classes in extracts of the midgut of Morimus funereus larvae. Zymogram analysis with gelatin as a peptidase substrate and phenylmethylsulfonyl fluoride as an inhibitor showed that serine peptidases were the most abundant endopeptidases in the midgut of M. funereus larvae. By zymogram analysis with gelatin as a peptidase substrate and 1,10-phenanthroline as an inhibitor, metallopeptidases were also detected. Analyses of serine peptidases with specific chromogenic substrates revealed dominance of elastase-like peptidases in extracts of the midgut of M. funereus larvae, with less pronounced chymotrypsin- and trypsin-like activities., Primenom specifičnih hromogenih supstrata, klasno-specifičnih inhibitora i zimogramske analize identifikovano je nekoliko klasa peptidaza u sirovom ekstraktu srednjeg creva larvi koleoptere Morimus funereus. Zimogramskom analizom sa želatinom kao supstratom i fenilmetilsulfonil-fluoridom kao inhibitorom utvrđeno je da su serin-peptidaze najzastupljenije peptidaze u ekstraktu srednjeg creva larvi M. funereus. Zimogramskom analizom sa želatinom kao supstratom i 1,10-fenantrolinom kaoinhibitorom takođe su detektovane metalopeptidaze. Analizom serin-peptidaza, upotrebom specifičnih hromogenih supstrata, dokazano je da su dominantni elastazi-slični enzimi u sirovom ekstraktu srednjeg creva larvi M. funereus, dok su himotripsinima- i tripsinima-slični enzimi manje zastupljeni.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae, Karakterizacija endopeptidaza srednjeg creva larvi Morimus funereus (Coleoptera: Cerambycidae)",
volume = "60",
number = "3",
pages = "403-409",
doi = "10.2298/ABS0803403B"
}

Božić, N., Dojnov, B., Milovanovic, A., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2008). Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 60(3), 403-409.
https://doi.org/10.2298/ABS0803403B

Božić N, Dojnov B, Milovanovic A, Nenadovic V, Ivanovic J, Vujčić Z. Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae. in Archives of biological sciences. 2008;60(3):403-409.
doi:10.2298/ABS0803403B .

Božić, Nataša, Dojnov, Biljana, Milovanovic, Aleksandra, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Characterization of endopeptidases from the midgut of Morimus funereus (Coleoptera : Cerambycidae) larvae" in Archives of biological sciences, 60, no. 3 (2008):403-409,
https://doi.org/10.2298/ABS0803403B . .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Božić, Nataša
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/923
AB  - Using soluble starch as a substrate five isoforms of alpha-amylase were identified in a crude extract of Morimus funereus larvae. The main alpha-amylase (termed AMF-3) was purified by gel filtration chromatography and anion exchange chromatography to obtain a single band on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Its enzymatic purity was confirmed by an in-gel activity assay after SDS-PAGE. The purity of AMF-3 was increased 112-fold with a 15.4% yield. AMF-3 had apparent molecular masses of 33 and 31 kDa when analysed using SDS-PAGE and Superdex 75 FPLC gel filtration chromatography, respectively and a calculated isoelectric point of 3.2. Purified AMF-3 showed maximal activity at pH 5.2 and had an optimum activity temperature of 45 degrees C. AMF-3 retained over 90% of its maximum activity at temperatures from 45 to 60 degrees C. AMF-3 exhibited a high affinity towards soluble starch with a K-m value of 0.43 mg/mL. Maximal AMF-3 activity was achieved in the presence of 0.1 mM CaCl2, while at higher concentrations its activity decreased. AMF-3 activity increased with increasing NaCl concentration. AMF-3 activity was significantly inhibited by alpha-amylase wheat inhibitor. Using a number of raw starch substrates maximum AMF-3 activity was achieved with horse-radish starch, in contrast to undetectable activity towards potato starch. (C) 2007 Elsevier Inc. All rights reserved.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
T1  - Purification and properties of midgut alpha-amylase isolated from Morimus funereus (Coleoptera : Cerambycidae) larvae
VL  - 149
IS  - 1
SP  - 153
EP  - 160
DO  - 10.1016/j.cbpb.2007.09.009
ER  - 

@article{
author = "Dojnov, Biljana and Božić, Nataša and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2008",
abstract = "Using soluble starch as a substrate five isoforms of alpha-amylase were identified in a crude extract of Morimus funereus larvae. The main alpha-amylase (termed AMF-3) was purified by gel filtration chromatography and anion exchange chromatography to obtain a single band on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Its enzymatic purity was confirmed by an in-gel activity assay after SDS-PAGE. The purity of AMF-3 was increased 112-fold with a 15.4% yield. AMF-3 had apparent molecular masses of 33 and 31 kDa when analysed using SDS-PAGE and Superdex 75 FPLC gel filtration chromatography, respectively and a calculated isoelectric point of 3.2. Purified AMF-3 showed maximal activity at pH 5.2 and had an optimum activity temperature of 45 degrees C. AMF-3 retained over 90% of its maximum activity at temperatures from 45 to 60 degrees C. AMF-3 exhibited a high affinity towards soluble starch with a K-m value of 0.43 mg/mL. Maximal AMF-3 activity was achieved in the presence of 0.1 mM CaCl2, while at higher concentrations its activity decreased. AMF-3 activity increased with increasing NaCl concentration. AMF-3 activity was significantly inhibited by alpha-amylase wheat inhibitor. Using a number of raw starch substrates maximum AMF-3 activity was achieved with horse-radish starch, in contrast to undetectable activity towards potato starch. (C) 2007 Elsevier Inc. All rights reserved.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology",
title = "Purification and properties of midgut alpha-amylase isolated from Morimus funereus (Coleoptera : Cerambycidae) larvae",
volume = "149",
number = "1",
pages = "153-160",
doi = "10.1016/j.cbpb.2007.09.009"
}

Dojnov, B., Božić, N., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2008). Purification and properties of midgut alpha-amylase isolated from Morimus funereus (Coleoptera : Cerambycidae) larvae. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 149(1), 153-160.
https://doi.org/10.1016/j.cbpb.2007.09.009

Dojnov B, Božić N, Nenadovic V, Ivanovic J, Vujčić Z. Purification and properties of midgut alpha-amylase isolated from Morimus funereus (Coleoptera : Cerambycidae) larvae. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology. 2008;149(1):153-160.
doi:10.1016/j.cbpb.2007.09.009 .

Dojnov, Biljana, Božić, Nataša, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Purification and properties of midgut alpha-amylase isolated from Morimus funereus (Coleoptera : Cerambycidae) larvae" in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 149, no. 1 (2008):153-160,
https://doi.org/10.1016/j.cbpb.2007.09.009 . .

TY  - JOUR
AU  - Božić, Nataša
AU  - Ivanovic, Jefisaveta
AU  - Nenadovic, Vera
AU  - Bergstroem, Joergen
AU  - Larsson, Thomas
AU  - Vujčić, Zoran
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/919
AB  - The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids in the active site, with the highest V-max /K-M ratio for leucine-p-nitroanilide (LpNA). Among a number of inhibitors tested, the most efficient were 1, 10-phenanthroline having a K-i value of 0.12 mM and cysteine with K-i value of 0.31 mM, while EGTA stimulated LAP activity. Zn2+, Mg2+ and Mn2+ all showed bi-modal effects on LAP activity (activated at low concentrations and inhibited at high concentrations). The purified LAP (after gel filtration on Superose 6 column) had molecular mass of 400 kDa with an isoelectric point of 6.2. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 67 kDa, suggesting that the enzyme is a hexamer. Six peptide sequences from protein band were obtained using ESI/MS-MS analysis. Comparison of the obtained peptide sequences with the EMBL-EBI sequence analysis toolbox and the BLASTP database showed a high degree of identity with other insect aminopeptidases. (C) 2007 Elsevier Inc. All rights reserved.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
T1  - Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae
VL  - 149
IS  - 3
SP  - 454
EP  - 462
DO  - 10.1016/j.cbpb.2007.11.006
ER  - 

@article{
author = "Božić, Nataša and Ivanovic, Jefisaveta and Nenadovic, Vera and Bergstroem, Joergen and Larsson, Thomas and Vujčić, Zoran",
year = "2008",
abstract = "The major leucyl aminopeptidase (LAP) from the midgut of Morimus funereus larvae was purified and characterised. Specific LAP activity was increased 292-fold by purification of the crude midgut extract. The purified enzyme had a pH optimum of 7.5 (optimum pH range 7.0-8.5) and preferentially hydrolysed p-nitroanilides containing hydrophobic amino acids in the active site, with the highest V-max /K-M ratio for leucine-p-nitroanilide (LpNA). Among a number of inhibitors tested, the most efficient were 1, 10-phenanthroline having a K-i value of 0.12 mM and cysteine with K-i value of 0.31 mM, while EGTA stimulated LAP activity. Zn2+, Mg2+ and Mn2+ all showed bi-modal effects on LAP activity (activated at low concentrations and inhibited at high concentrations). The purified LAP (after gel filtration on Superose 6 column) had molecular mass of 400 kDa with an isoelectric point of 6.2. Sodium dodecylsulphate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed one band of 67 kDa, suggesting that the enzyme is a hexamer. Six peptide sequences from protein band were obtained using ESI/MS-MS analysis. Comparison of the obtained peptide sequences with the EMBL-EBI sequence analysis toolbox and the BLASTP database showed a high degree of identity with other insect aminopeptidases. (C) 2007 Elsevier Inc. All rights reserved.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology",
title = "Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae",
volume = "149",
number = "3",
pages = "454-462",
doi = "10.1016/j.cbpb.2007.11.006"
}

Božić, N., Ivanovic, J., Nenadovic, V., Bergstroem, J., Larsson, T.,& Vujčić, Z.. (2008). Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 149(3), 454-462.
https://doi.org/10.1016/j.cbpb.2007.11.006

Božić N, Ivanovic J, Nenadovic V, Bergstroem J, Larsson T, Vujčić Z. Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology. 2008;149(3):454-462.
doi:10.1016/j.cbpb.2007.11.006 .

Božić, Nataša, Ivanovic, Jefisaveta, Nenadovic, Vera, Bergstroem, Joergen, Larsson, Thomas, Vujčić, Zoran, "Purification and properties of major midgut leucyl aminopeptidase of Morimus funereus (Coleoptera, Cerambycidae) larvae" in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 149, no. 3 (2008):454-462,
https://doi.org/10.1016/j.cbpb.2007.11.006 . .

TY  - JOUR
AU  - Todorović, Tamara
AU  - Bacchi, Alessia
AU  - Juranic, Nenad O.
AU  - Sladić, Dušan
AU  - Pelizzi, Giancarlo
AU  - Božić, Tatjana T.
AU  - Filipović, Nenad R.
AU  - Anđelković, Katarina K.
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/859
AB  - New complexes of Cd(II), Zn(II) and Ni(II) with 2-quinolinecarboxaldehyde selenosernicarbazone (Hqasesc) were synthesized and structurally characterized. The structure of the ligand, Cd(II) and Zn(II) complexes was determined by NMR and IR spectroscopy, elemental microanalysis and molar conductivity measurements. Both complexes occur in solution in two forms, the major tetrahedral and minor octahedral. In the major Cd(II) complex one qasesc(-) ligand is coordinated as a tridentate, the fourth coordination site being occupied by acetate, while in the major Zn(II) complex two qasesc- ligands are coordinated as bidentates. In both minor complexes two qasesc- ligands are coordinated as tridentates forming the octahedral geometry around the central metal ion. The only paramagnetic complex in the series is Ni(II) complex for which X-ray structure analysis was performed. The complex has the angularly distorted octahedral geometry with two qasesc- ligands coordinated as tridentates, in a similar way as in the minor complexes of Cd(11) and Zn(11). (c) 2007 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Polyhedron
T1  - Synthesis and characterization of novel Cd(II), Zn(II) and Ni(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone. Crystal structure of bis(2-quinolinecarboxaldehyde selenosemicarbazonato)nickel(II)
VL  - 26
IS  - 13
SP  - 3428
EP  - 3436
DO  - 10.1016/j.poly.2007.03.023
ER  - 

@article{
author = "Todorović, Tamara and Bacchi, Alessia and Juranic, Nenad O. and Sladić, Dušan and Pelizzi, Giancarlo and Božić, Tatjana T. and Filipović, Nenad R. and Anđelković, Katarina K.",
year = "2007",
abstract = "New complexes of Cd(II), Zn(II) and Ni(II) with 2-quinolinecarboxaldehyde selenosernicarbazone (Hqasesc) were synthesized and structurally characterized. The structure of the ligand, Cd(II) and Zn(II) complexes was determined by NMR and IR spectroscopy, elemental microanalysis and molar conductivity measurements. Both complexes occur in solution in two forms, the major tetrahedral and minor octahedral. In the major Cd(II) complex one qasesc(-) ligand is coordinated as a tridentate, the fourth coordination site being occupied by acetate, while in the major Zn(II) complex two qasesc- ligands are coordinated as bidentates. In both minor complexes two qasesc- ligands are coordinated as tridentates forming the octahedral geometry around the central metal ion. The only paramagnetic complex in the series is Ni(II) complex for which X-ray structure analysis was performed. The complex has the angularly distorted octahedral geometry with two qasesc- ligands coordinated as tridentates, in a similar way as in the minor complexes of Cd(11) and Zn(11). (c) 2007 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Polyhedron",
title = "Synthesis and characterization of novel Cd(II), Zn(II) and Ni(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone. Crystal structure of bis(2-quinolinecarboxaldehyde selenosemicarbazonato)nickel(II)",
volume = "26",
number = "13",
pages = "3428-3436",
doi = "10.1016/j.poly.2007.03.023"
}

Todorović, T., Bacchi, A., Juranic, N. O., Sladić, D., Pelizzi, G., Božić, T. T., Filipović, N. R.,& Anđelković, K. K.. (2007). Synthesis and characterization of novel Cd(II), Zn(II) and Ni(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone. Crystal structure of bis(2-quinolinecarboxaldehyde selenosemicarbazonato)nickel(II). in Polyhedron
Pergamon-Elsevier Science Ltd, Oxford., 26(13), 3428-3436.
https://doi.org/10.1016/j.poly.2007.03.023

Todorović T, Bacchi A, Juranic NO, Sladić D, Pelizzi G, Božić TT, Filipović NR, Anđelković KK. Synthesis and characterization of novel Cd(II), Zn(II) and Ni(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone. Crystal structure of bis(2-quinolinecarboxaldehyde selenosemicarbazonato)nickel(II). in Polyhedron. 2007;26(13):3428-3436.
doi:10.1016/j.poly.2007.03.023 .

Todorović, Tamara, Bacchi, Alessia, Juranic, Nenad O., Sladić, Dušan, Pelizzi, Giancarlo, Božić, Tatjana T., Filipović, Nenad R., Anđelković, Katarina K., "Synthesis and characterization of novel Cd(II), Zn(II) and Ni(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone. Crystal structure of bis(2-quinolinecarboxaldehyde selenosemicarbazonato)nickel(II)" in Polyhedron, 26, no. 13 (2007):3428-3436,
https://doi.org/10.1016/j.poly.2007.03.023 . .

TY  - CONF
AU  - Filipović, Nenad R.
AU  - Todorović, Tamara
AU  - Sladić, Dušan
AU  - Novaković, Irena T.
AU  - Jeremić, Dejan
AU  - Anđelković, Katarina K.
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/866
AB  - New complexes of Pt(II) with condensation derivatives of ethyl hydrazino acetate and either 2-acetylpyridine or 2-quinolinecarboxaldehyde, and of Pd(II) with the condensation derivative of ethyl hydrazinoacetate and 2-quinolinecarboxaldehyde were synthesized and characterized by elemental analysis, IR, H-1- and C-13-NMR spectroscopy, and molar conductivity measurements. The complexes have a square planar geometry, ligands binding as bidentates in the neutral form, and the remaining two coordination sites being occupied by chloride ions. Biological activity of new complexes, and of previously synthesized Pd(II), Cd(II), Co(III) and Zn(II) complexes with this ligand type was evaluated by the brine shrimp test. All the complexes showed a moderate activity.
PB  - Trans Tech Publications Ltd, Durnten-Zurich
C3  - Materials Science Forum
T1  - Synthesis, characterization and biological activity evaluation of novel Pd(II) and Pt(II) complexes with heterocyclic hydrazone ligands
VL  - 555
SP  - 423
EP  - 427
DO  - 10.4028/www.scientific.net/MSF.555.423
ER  - 

@conference{
author = "Filipović, Nenad R. and Todorović, Tamara and Sladić, Dušan and Novaković, Irena T. and Jeremić, Dejan and Anđelković, Katarina K.",
year = "2007",
abstract = "New complexes of Pt(II) with condensation derivatives of ethyl hydrazino acetate and either 2-acetylpyridine or 2-quinolinecarboxaldehyde, and of Pd(II) with the condensation derivative of ethyl hydrazinoacetate and 2-quinolinecarboxaldehyde were synthesized and characterized by elemental analysis, IR, H-1- and C-13-NMR spectroscopy, and molar conductivity measurements. The complexes have a square planar geometry, ligands binding as bidentates in the neutral form, and the remaining two coordination sites being occupied by chloride ions. Biological activity of new complexes, and of previously synthesized Pd(II), Cd(II), Co(III) and Zn(II) complexes with this ligand type was evaluated by the brine shrimp test. All the complexes showed a moderate activity.",
publisher = "Trans Tech Publications Ltd, Durnten-Zurich",
journal = "Materials Science Forum",
title = "Synthesis, characterization and biological activity evaluation of novel Pd(II) and Pt(II) complexes with heterocyclic hydrazone ligands",
volume = "555",
pages = "423-427",
doi = "10.4028/www.scientific.net/MSF.555.423"
}

Filipović, N. R., Todorović, T., Sladić, D., Novaković, I. T., Jeremić, D.,& Anđelković, K. K.. (2007). Synthesis, characterization and biological activity evaluation of novel Pd(II) and Pt(II) complexes with heterocyclic hydrazone ligands. in Materials Science Forum
Trans Tech Publications Ltd, Durnten-Zurich., 555, 423-427.
https://doi.org/10.4028/www.scientific.net/MSF.555.423

Filipović NR, Todorović T, Sladić D, Novaković IT, Jeremić D, Anđelković KK. Synthesis, characterization and biological activity evaluation of novel Pd(II) and Pt(II) complexes with heterocyclic hydrazone ligands. in Materials Science Forum. 2007;555:423-427.
doi:10.4028/www.scientific.net/MSF.555.423 .

Filipović, Nenad R., Todorović, Tamara, Sladić, Dušan, Novaković, Irena T., Jeremić, Dejan, Anđelković, Katarina K., "Synthesis, characterization and biological activity evaluation of novel Pd(II) and Pt(II) complexes with heterocyclic hydrazone ligands" in Materials Science Forum, 555 (2007):423-427,
https://doi.org/10.4028/www.scientific.net/MSF.555.423 . .

TY  - JOUR
AU  - Pajic, Ivana
AU  - Vujčić, Zoran
AU  - Vujčić, Miroslava
AU  - Novaković, Irena T.
AU  - Sladić, Dušan
AU  - Gasic, Miroslav J.
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/906
AB  - The quinone avarone, isolated from the marine sponge Dysidea avara, possesses the ability to chemically modify proteins. In this work, modification of lectin isolated from the coral Gerardia savaglia by avarone was examined. The techniques used for studying the modification were: SDS PAGE, isoelectric focusing and hemagglutination testing. The results of the SDS PAGE indicate dimerization of the protein. A shift of the pI toward lower value occurs upon modification. The change of the hemagglutination activity of the protein confirms that chemical modification of G. savaglia lectin by avarone changes its ability to interact with the membrane of erythrocytes.
AB  - Avaron, hinon izolovan iz morskog sunđera Dysidea avara, poseduje sposobnost da hemijski modifikuje proteine. U ovom radu ispitivana je modifikacija lektina izolovanog iz korala Gerardia savaglia avaronom. Tehnike za praćenje hemijske modifikacije bile su: SDS PAGE, izoelektrično fokusiranje i hemaglutinacioni test. Rezultati SDS PAGE upućuju na dimerizaciju proteina. Dolazi do pomeranja pI vrednosti proteina. Promena hemaglutinacione aktivnosti G. savaglia lektina avaronom uticala je na njegovu sposobnost interakcije sa membranom eritrocita.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Chemical modification of the lectin of the marine coral Gerardia savaglia by marine quinone avarone
T1  - Hemijske modifikacije lektina morskog korala Gerardia savaglia morskim hinonom avaronom
VL  - 72
IS  - 12
SP  - 1271
EP  - 1274
DO  - 10.2298/JSC0712271P
ER  - 

@article{
author = "Pajic, Ivana and Vujčić, Zoran and Vujčić, Miroslava and Novaković, Irena T. and Sladić, Dušan and Gasic, Miroslav J.",
year = "2007",
abstract = "The quinone avarone, isolated from the marine sponge Dysidea avara, possesses the ability to chemically modify proteins. In this work, modification of lectin isolated from the coral Gerardia savaglia by avarone was examined. The techniques used for studying the modification were: SDS PAGE, isoelectric focusing and hemagglutination testing. The results of the SDS PAGE indicate dimerization of the protein. A shift of the pI toward lower value occurs upon modification. The change of the hemagglutination activity of the protein confirms that chemical modification of G. savaglia lectin by avarone changes its ability to interact with the membrane of erythrocytes., Avaron, hinon izolovan iz morskog sunđera Dysidea avara, poseduje sposobnost da hemijski modifikuje proteine. U ovom radu ispitivana je modifikacija lektina izolovanog iz korala Gerardia savaglia avaronom. Tehnike za praćenje hemijske modifikacije bile su: SDS PAGE, izoelektrično fokusiranje i hemaglutinacioni test. Rezultati SDS PAGE upućuju na dimerizaciju proteina. Dolazi do pomeranja pI vrednosti proteina. Promena hemaglutinacione aktivnosti G. savaglia lektina avaronom uticala je na njegovu sposobnost interakcije sa membranom eritrocita.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical modification of the lectin of the marine coral Gerardia savaglia by marine quinone avarone, Hemijske modifikacije lektina morskog korala Gerardia savaglia morskim hinonom avaronom",
volume = "72",
number = "12",
pages = "1271-1274",
doi = "10.2298/JSC0712271P"
}

Pajic, I., Vujčić, Z., Vujčić, M., Novaković, I. T., Sladić, D.,& Gasic, M. J.. (2007). Chemical modification of the lectin of the marine coral Gerardia savaglia by marine quinone avarone. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 72(12), 1271-1274.
https://doi.org/10.2298/JSC0712271P

Pajic I, Vujčić Z, Vujčić M, Novaković IT, Sladić D, Gasic MJ. Chemical modification of the lectin of the marine coral Gerardia savaglia by marine quinone avarone. in Journal of the Serbian Chemical Society. 2007;72(12):1271-1274.
doi:10.2298/JSC0712271P .

Pajic, Ivana, Vujčić, Zoran, Vujčić, Miroslava, Novaković, Irena T., Sladić, Dušan, Gasic, Miroslav J., "Chemical modification of the lectin of the marine coral Gerardia savaglia by marine quinone avarone" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1271-1274,
https://doi.org/10.2298/JSC0712271P . .

TY  - JOUR
AU  - Vujčić, Miroslava
AU  - Tufegdžić, Srđan
AU  - Vujčić, Zoran
AU  - Gasic, Miroslav J.
AU  - Sladić, Dušan
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/905
AB  - Changes in electrophoresis pattern after interaction of supercoiled plasmid pBR322 DNA with avarol was studied at a micromolar concentration of reactants under mild reaction conditions. Interactions of avarol with linear high-molecular CT-DNA at millimolar concentrations were analyzed by electrophoresis and UV spectrophotometry. It was observed that avarol is capable of quenching ethidium bromide fluorescence in DNA bands. An increase in the absorbance of DNA was detected. The results indicate the binding of avarol to DNA and/or modification of nucleotide bases.
AB  - Proučavane su promene elektroforetskog ponašanja DNA posle interakcija superhelikoidalnog plazmida pBR322 s avarolom pri mikromolarnim koncentracijama reaktanata pod blagim reakcionim uslovima. Interakcije avarola sa linearnom visokomolekulskom CT-DNA pri milimolarnim koncentracijama analizirane su elektroforezom i UV spektrofotometrijom. Uočeno je da je avarol u stanju da gasi fluorescenciju etidijum-bromida u trakama koje potiču od DNA. Detektovan je porast apsorbancije DNA. Rezultati ukazuju na vezivanje avarona za DNA i/ili modifikaciju nukleotidnih baza.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Interactions of the anti-tumor sesquiterpene hydroquinone avarol with DNA in vitro
T1  - Interakcije antitumorskog seskviterpenskog hidrohinona avarola sa DNA in vitro
VL  - 72
IS  - 12
SP  - 1265
EP  - 1269
DO  - 10.2298/JSC0712265V
ER  - 

@article{
author = "Vujčić, Miroslava and Tufegdžić, Srđan and Vujčić, Zoran and Gasic, Miroslav J. and Sladić, Dušan",
year = "2007",
abstract = "Changes in electrophoresis pattern after interaction of supercoiled plasmid pBR322 DNA with avarol was studied at a micromolar concentration of reactants under mild reaction conditions. Interactions of avarol with linear high-molecular CT-DNA at millimolar concentrations were analyzed by electrophoresis and UV spectrophotometry. It was observed that avarol is capable of quenching ethidium bromide fluorescence in DNA bands. An increase in the absorbance of DNA was detected. The results indicate the binding of avarol to DNA and/or modification of nucleotide bases., Proučavane su promene elektroforetskog ponašanja DNA posle interakcija superhelikoidalnog plazmida pBR322 s avarolom pri mikromolarnim koncentracijama reaktanata pod blagim reakcionim uslovima. Interakcije avarola sa linearnom visokomolekulskom CT-DNA pri milimolarnim koncentracijama analizirane su elektroforezom i UV spektrofotometrijom. Uočeno je da je avarol u stanju da gasi fluorescenciju etidijum-bromida u trakama koje potiču od DNA. Detektovan je porast apsorbancije DNA. Rezultati ukazuju na vezivanje avarona za DNA i/ili modifikaciju nukleotidnih baza.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Interactions of the anti-tumor sesquiterpene hydroquinone avarol with DNA in vitro, Interakcije antitumorskog seskviterpenskog hidrohinona avarola sa DNA in vitro",
volume = "72",
number = "12",
pages = "1265-1269",
doi = "10.2298/JSC0712265V"
}

Vujčić, M., Tufegdžić, S., Vujčić, Z., Gasic, M. J.,& Sladić, D.. (2007). Interactions of the anti-tumor sesquiterpene hydroquinone avarol with DNA in vitro. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 72(12), 1265-1269.
https://doi.org/10.2298/JSC0712265V

Vujčić M, Tufegdžić S, Vujčić Z, Gasic MJ, Sladić D. Interactions of the anti-tumor sesquiterpene hydroquinone avarol with DNA in vitro. in Journal of the Serbian Chemical Society. 2007;72(12):1265-1269.
doi:10.2298/JSC0712265V .

Vujčić, Miroslava, Tufegdžić, Srđan, Vujčić, Zoran, Gasic, Miroslav J., Sladić, Dušan, "Interactions of the anti-tumor sesquiterpene hydroquinone avarol with DNA in vitro" in Journal of the Serbian Chemical Society, 72, no. 12 (2007):1265-1269,
https://doi.org/10.2298/JSC0712265V . .

TY  - JOUR
AU  - Milovanovic, Aleksandra
AU  - Božić, Nataša
AU  - Vujčić, Zoran
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/831
AB  - Yeast cell wall invertase (CWI) was immobilized within calcium alginate beads. The result of entrapment was the complete immobilization of all the added CWI. Three types of biocatalysts were prepared: CWI-S, CWI-155 and CWI-157. The optimum pH values were 4.5 and 5.0 for free and immobilized invertase, respectively. The optimum temperature was 60 degrees C, for both free CWI and CWI-S immobilizate. 80 degrees C was the optimum temperature for CWI-155 whereas the optimum temperature for CWI-157 ranged from 50 degrees C to 80 degrees C. Immobilized CWI was more stable than was free CWI above optimum activity temperatures. The activation energies were 32 kJ/mol for free CWI and 45, 21 and 25 kJ/mol for CWI-S, CWI-155 and CWI-157, respectively. The Km values of free and immobilized CWI-157 were 28.4 mM and 72 mM, respectively. The V-max values were estimated as 4.5 mM/min and 0.42 mM/min, respectively. Immobilized CWI-157 was tested in a batch reactor using 70% sucrose (w/v). Complete sucrose conversion was achieved after 55 h. After 40 consecutive cycles, CWI-157 retained 90% of its activity. (c) 2006 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Cell wall invertase immobilization within calcium alginate beads
VL  - 104
IS  - 1
SP  - 81
EP  - 86
DO  - 10.1016/j.foodchem.2006.11.001
ER  - 

@article{
author = "Milovanovic, Aleksandra and Božić, Nataša and Vujčić, Zoran",
year = "2007",
abstract = "Yeast cell wall invertase (CWI) was immobilized within calcium alginate beads. The result of entrapment was the complete immobilization of all the added CWI. Three types of biocatalysts were prepared: CWI-S, CWI-155 and CWI-157. The optimum pH values were 4.5 and 5.0 for free and immobilized invertase, respectively. The optimum temperature was 60 degrees C, for both free CWI and CWI-S immobilizate. 80 degrees C was the optimum temperature for CWI-155 whereas the optimum temperature for CWI-157 ranged from 50 degrees C to 80 degrees C. Immobilized CWI was more stable than was free CWI above optimum activity temperatures. The activation energies were 32 kJ/mol for free CWI and 45, 21 and 25 kJ/mol for CWI-S, CWI-155 and CWI-157, respectively. The Km values of free and immobilized CWI-157 were 28.4 mM and 72 mM, respectively. The V-max values were estimated as 4.5 mM/min and 0.42 mM/min, respectively. Immobilized CWI-157 was tested in a batch reactor using 70% sucrose (w/v). Complete sucrose conversion was achieved after 55 h. After 40 consecutive cycles, CWI-157 retained 90% of its activity. (c) 2006 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Cell wall invertase immobilization within calcium alginate beads",
volume = "104",
number = "1",
pages = "81-86",
doi = "10.1016/j.foodchem.2006.11.001"
}

Milovanovic, A., Božić, N.,& Vujčić, Z.. (2007). Cell wall invertase immobilization within calcium alginate beads. in Food Chemistry
Elsevier Sci Ltd, Oxford., 104(1), 81-86.
https://doi.org/10.1016/j.foodchem.2006.11.001

Milovanovic A, Božić N, Vujčić Z. Cell wall invertase immobilization within calcium alginate beads. in Food Chemistry. 2007;104(1):81-86.
doi:10.1016/j.foodchem.2006.11.001 .

Milovanovic, Aleksandra, Božić, Nataša, Vujčić, Zoran, "Cell wall invertase immobilization within calcium alginate beads" in Food Chemistry, 104, no. 1 (2007):81-86,
https://doi.org/10.1016/j.foodchem.2006.11.001 . .

TY  - JOUR
AU  - Dojnov, Bijana
AU  - Božić, Nataša
AU  - Bulajic, Nina
AU  - Vujčić, Zoran
PY  - 2007
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/895
AB  - Immunoblot analysis is not in wide use for diagnosis of invasive candidiasis, mostly because the procedure is not standardized and hence not reliable. This work describes a standardized method for C. albicans antigen extract preparation and immuno-chemical detection. The major improvement of the method is the preparation of combined antigen extract-consisting of the cell wall and cytosol antigens. The fungal cells and lysis buffer were mixed at a 1:3 ratio and disintegrated by ultrasound for six cycles of one minute each. After centrifugation, cytosol antigens were obtained in the supernatant and cell wall antigens were in the precipitate. Precipitate was dissolved in lysis buffer with 2% sodium doclecyl sulfate (SDS) and boiled at 100 degrees C for 2min. After centrifugation, the supernatant was combined with the previous one, so the extract of the combined antigens was obtained in the mixture. With those combined antigen extracts and with sera of three different groups of patients, immunoblot analysis showed sensitivity of 90.2%, specificity of 84.4%, and accuracy of 88.0%.
PB  - Wiley-Liss, Hoboken
T2  - Journal of Clinical Laboratory Analysis
T1  - Preparation of combined extract of cell wall and cytosol antigens of Candida albicans for immunoblot analysis
VL  - 21
IS  - 6
SP  - 406
EP  - 412
DO  - 10.1002/jcla.20206
ER  - 

@article{
author = "Dojnov, Bijana and Božić, Nataša and Bulajic, Nina and Vujčić, Zoran",
year = "2007",
abstract = "Immunoblot analysis is not in wide use for diagnosis of invasive candidiasis, mostly because the procedure is not standardized and hence not reliable. This work describes a standardized method for C. albicans antigen extract preparation and immuno-chemical detection. The major improvement of the method is the preparation of combined antigen extract-consisting of the cell wall and cytosol antigens. The fungal cells and lysis buffer were mixed at a 1:3 ratio and disintegrated by ultrasound for six cycles of one minute each. After centrifugation, cytosol antigens were obtained in the supernatant and cell wall antigens were in the precipitate. Precipitate was dissolved in lysis buffer with 2% sodium doclecyl sulfate (SDS) and boiled at 100 degrees C for 2min. After centrifugation, the supernatant was combined with the previous one, so the extract of the combined antigens was obtained in the mixture. With those combined antigen extracts and with sera of three different groups of patients, immunoblot analysis showed sensitivity of 90.2%, specificity of 84.4%, and accuracy of 88.0%.",
publisher = "Wiley-Liss, Hoboken",
journal = "Journal of Clinical Laboratory Analysis",
title = "Preparation of combined extract of cell wall and cytosol antigens of Candida albicans for immunoblot analysis",
volume = "21",
number = "6",
pages = "406-412",
doi = "10.1002/jcla.20206"
}

Dojnov, B., Božić, N., Bulajic, N.,& Vujčić, Z.. (2007). Preparation of combined extract of cell wall and cytosol antigens of Candida albicans for immunoblot analysis. in Journal of Clinical Laboratory Analysis
Wiley-Liss, Hoboken., 21(6), 406-412.
https://doi.org/10.1002/jcla.20206

Dojnov B, Božić N, Bulajic N, Vujčić Z. Preparation of combined extract of cell wall and cytosol antigens of Candida albicans for immunoblot analysis. in Journal of Clinical Laboratory Analysis. 2007;21(6):406-412.
doi:10.1002/jcla.20206 .

Dojnov, Bijana, Božić, Nataša, Bulajic, Nina, Vujčić, Zoran, "Preparation of combined extract of cell wall and cytosol antigens of Candida albicans for immunoblot analysis" in Journal of Clinical Laboratory Analysis, 21, no. 6 (2007):406-412,
https://doi.org/10.1002/jcla.20206 . .