TY  - JOUR
AU  - Dojnov, Biljana
AU  - Pavlovic, Ratko
AU  - Božić, Nataša
AU  - Margetić, Aleksandra
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2013
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1627
AB  - The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut.
PB  - Elsevier Science Inc, New York
T2  - Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
T1  - Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition
VL  - 164
IS  - 4
SP  - 259
EP  - 267
DO  - 10.1016/j.cbpb.2013.02.001
ER  - 

@article{
author = "Dojnov, Biljana and Pavlovic, Ratko and Božić, Nataša and Margetić, Aleksandra and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2013",
abstract = "The influence of diet composition - two substrates, wheat bran and sawdust - on isoform expression of digestive enzymes (cellulase, amylase and peptidase) in the midgut of Morimus funereus larvae was examined. Their impact on larval development was demonstrated by measuring the increase of larval weight during development and by analysis of digestive enzymes zymographic profiles, where the expression of cellulase isoforms from M. funereus larvae midgut has been examined for the first time in this study. Larvae reared on wheat bran had higher body weight between day 60 and day 100 than larvae reared on sawdust; however, both groups achieved similar body weight after day 110. Wheat bran as substrate induced different cellulase and amylase isoforms. Oak sawdust in substrate acted as inducer of peptidases. The highest cellulase activity and the greatest isoform variability were detected in the midgut extracts of larvae reared on wheat bran. From our results it can be assumed that M. funereus endocellulase, amylase and peptidase are secreted in the anterior midgut, and their concentration gradually decreases towards the hindgut.",
publisher = "Elsevier Science Inc, New York",
journal = "Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology",
title = "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition",
volume = "164",
number = "4",
pages = "259-267",
doi = "10.1016/j.cbpb.2013.02.001"
}

Dojnov, B., Pavlovic, R., Božić, N., Margetić, A., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2013). Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology
Elsevier Science Inc, New York., 164(4), 259-267.
https://doi.org/10.1016/j.cbpb.2013.02.001

Dojnov B, Pavlovic R, Božić N, Margetić A, Nenadovic V, Ivanovic J, Vujčić Z. Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition. in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology. 2013;164(4):259-267.
doi:10.1016/j.cbpb.2013.02.001 .

Dojnov, Biljana, Pavlovic, Ratko, Božić, Nataša, Margetić, Aleksandra, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Expression and distribution of cellulase, amylase and peptidase isoforms along the midgut of Morimus funereus L. (Coleoptera: Cerambycidae) larvae is dependent on nutrient substrate composition" in Comparative Biochemistry and Physiology. B: Biochemistry and Molecular Biology, 164, no. 4 (2013):259-267,
https://doi.org/10.1016/j.cbpb.2013.02.001 . .

TY  - JOUR
AU  - Dojnov, Biljana
AU  - Vujčić, Zoran
AU  - Božić, Nataša
AU  - Margetić, Aleksandra
AU  - Vujčić, Miroslava
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1263
AB  - Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.
PB  - Springer, Dordrecht
T2  - Journal of Insect Conservation
T1  - Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study
VL  - 16
IS  - 2
SP  - 239
EP  - 247
DO  - 10.1007/s10841-011-9411-x
ER  - 

@article{
author = "Dojnov, Biljana and Vujčić, Zoran and Božić, Nataša and Margetić, Aleksandra and Vujčić, Miroslava and Nenadovic, Vera and Ivanovic, Jelisaveta",
year = "2012",
abstract = "Captive breeding has been suggested as a method of conservation for many vertebrates, and is increasingly being proposed as a strategy for invertebrates. In this study, the growth, development and fertility of adults of the vulnerable cerambycid Morimus funereus reared in captivity are examined. Two oviposition cycles; from May to September and from January to March were studied and larvae from wild adults and from the progeny of captive adults (second generation larvae) were examined. Five to 12 instars were observed during larval development. Larval development was completed in 218 days (average) for the progeny of wild adults with an average mortality rate of 10.3% and in 226 days (average) for larvae from captive adults with mortality rate of 34.9%. First generation larval body weights were disparate during development, while second generation larvae had similar weights with no significant differences. In this study we have tested the potential of captive breaded M. funereus larvae as a model for investigation of digestive enzymes. Amylase from the midgut of larvae reared under laboratory conditions showed twofold higher specific activities with a decreased number of isoforms expressed, as compared to the enzyme from field-collected larvae. Captive breeding of M. funereus can be used in the future as a part of an effective conservation strategy for this rare insect species.",
publisher = "Springer, Dordrecht",
journal = "Journal of Insect Conservation",
title = "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study",
volume = "16",
number = "2",
pages = "239-247",
doi = "10.1007/s10841-011-9411-x"
}

Dojnov, B., Vujčić, Z., Božić, N., Margetić, A., Vujčić, M., Nenadovic, V.,& Ivanovic, J.. (2012). Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation
Springer, Dordrecht., 16(2), 239-247.
https://doi.org/10.1007/s10841-011-9411-x

Dojnov B, Vujčić Z, Božić N, Margetić A, Vujčić M, Nenadovic V, Ivanovic J. Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study. in Journal of Insect Conservation. 2012;16(2):239-247.
doi:10.1007/s10841-011-9411-x .

Dojnov, Biljana, Vujčić, Zoran, Božić, Nataša, Margetić, Aleksandra, Vujčić, Miroslava, Nenadovic, Vera, Ivanovic, Jelisaveta, "Adaptations to captive breeding of the longhorn beetle Morimus funereus (Coleoptera: Cerambycidae); application on amylase study" in Journal of Insect Conservation, 16, no. 2 (2012):239-247,
https://doi.org/10.1007/s10841-011-9411-x . .

TY  - JOUR
AU  - Pavlovic, R.
AU  - Grujić, Marica
AU  - Dojnov, Biljana
AU  - Vujčić, Miroslava
AU  - Nenadovic, Vera
AU  - Ivanovic, Jelisaveta
AU  - Vujčić, Zoran
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1300
AB  - The expression and distribution of digestive cellulases along the midgut of Cerambyx cerdo larvae were analyzed for the first time and are presented in this article. Four groups of larvae were examined: larvae developed in the wild; larvae taken from the wild and successively reared on an artificial diet based on polenta; and larvae hatched in the laboratory and reared on two different artificial diets. Seven endocellulase and seven beta-D-glucosidase isoforms were detected in all midgut extracts of C. cerdo with a zymogram after native PAGE. We observed that C. cerdo larvae are capable of producing cellulase isoforms with different PAGE mobilities depending on the nutrient substrate. From our findings it can be assumed that, depending on the distribution of endocellulase and beta-D-glucosidase, cellulose molecules are first fragmented in the anterior and middle midgut by endo-beta-1,4-glucanase; subsequently, the obtained fragments are broken down by beta-D-glucosidase mostly in middle midgut.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Influence of Nutrient Substrates on the Expression of Cellulases in Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae
VL  - 64
IS  - 2
SP  - 757
EP  - 765
DO  - 10.2298/ABS1202757P
ER  - 

@article{
author = "Pavlovic, R. and Grujić, Marica and Dojnov, Biljana and Vujčić, Miroslava and Nenadovic, Vera and Ivanovic, Jelisaveta and Vujčić, Zoran",
year = "2012",
abstract = "The expression and distribution of digestive cellulases along the midgut of Cerambyx cerdo larvae were analyzed for the first time and are presented in this article. Four groups of larvae were examined: larvae developed in the wild; larvae taken from the wild and successively reared on an artificial diet based on polenta; and larvae hatched in the laboratory and reared on two different artificial diets. Seven endocellulase and seven beta-D-glucosidase isoforms were detected in all midgut extracts of C. cerdo with a zymogram after native PAGE. We observed that C. cerdo larvae are capable of producing cellulase isoforms with different PAGE mobilities depending on the nutrient substrate. From our findings it can be assumed that, depending on the distribution of endocellulase and beta-D-glucosidase, cellulose molecules are first fragmented in the anterior and middle midgut by endo-beta-1,4-glucanase; subsequently, the obtained fragments are broken down by beta-D-glucosidase mostly in middle midgut.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Influence of Nutrient Substrates on the Expression of Cellulases in Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae",
volume = "64",
number = "2",
pages = "757-765",
doi = "10.2298/ABS1202757P"
}

Pavlovic, R., Grujić, M., Dojnov, B., Vujčić, M., Nenadovic, V., Ivanovic, J.,& Vujčić, Z.. (2012). Influence of Nutrient Substrates on the Expression of Cellulases in Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 64(2), 757-765.
https://doi.org/10.2298/ABS1202757P

Pavlovic R, Grujić M, Dojnov B, Vujčić M, Nenadovic V, Ivanovic J, Vujčić Z. Influence of Nutrient Substrates on the Expression of Cellulases in Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae. in Archives of biological sciences. 2012;64(2):757-765.
doi:10.2298/ABS1202757P .

Pavlovic, R., Grujić, Marica, Dojnov, Biljana, Vujčić, Miroslava, Nenadovic, Vera, Ivanovic, Jelisaveta, Vujčić, Zoran, "Influence of Nutrient Substrates on the Expression of Cellulases in Cerambyx Cerdo L. (Coleoptera: Cerambycidae) Larvae" in Archives of biological sciences, 64, no. 2 (2012):757-765,
https://doi.org/10.2298/ABS1202757P . .

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  - 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 . .