Krstić, Dijana

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Authority KeyName Variants
8980c32d-a714-47b5-9aae-7dd0f5a9911d
  • Krstić, Dijana (2)
  • Krstić, Danijela (1)
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Author's Bibliography

Xanthones and C-glucosides from the aerial parts of four species of Gentianella from Serbia and Montenegro

Jankovic, T; Krstić, Dijana; Aljančić, Ivana; Savikin-Fodulovic, K; Menković, N.; Vajs, Vlatka; Milosavljevic, S

(Pergamon-Elsevier Science Ltd, Oxford, 2005)

TY  - JOUR
AU  - Jankovic, T
AU  - Krstić, Dijana
AU  - Aljančić, Ivana
AU  - Savikin-Fodulovic, K
AU  - Menković, N.
AU  - Vajs, Vlatka
AU  - Milosavljevic, S
PY  - 2005
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/710
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Biochemical Systematics and Ecology
T1  - Xanthones and C-glucosides from the aerial parts of four species of Gentianella from Serbia and Montenegro
VL  - 33
IS  - 7
SP  - 729
EP  - 735
DO  - 10.1016/j.bse.2004.12.010
ER  - 
@article{
author = "Jankovic, T and Krstić, Dijana and Aljančić, Ivana and Savikin-Fodulovic, K and Menković, N. and Vajs, Vlatka and Milosavljevic, S",
year = "2005",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Biochemical Systematics and Ecology",
title = "Xanthones and C-glucosides from the aerial parts of four species of Gentianella from Serbia and Montenegro",
volume = "33",
number = "7",
pages = "729-735",
doi = "10.1016/j.bse.2004.12.010"
}
Jankovic, T., Krstić, D., Aljančić, I., Savikin-Fodulovic, K., Menković, N., Vajs, V.,& Milosavljevic, S.. (2005). Xanthones and C-glucosides from the aerial parts of four species of Gentianella from Serbia and Montenegro. in Biochemical Systematics and Ecology
Pergamon-Elsevier Science Ltd, Oxford., 33(7), 729-735.
https://doi.org/10.1016/j.bse.2004.12.010
Jankovic T, Krstić D, Aljančić I, Savikin-Fodulovic K, Menković N, Vajs V, Milosavljevic S. Xanthones and C-glucosides from the aerial parts of four species of Gentianella from Serbia and Montenegro. in Biochemical Systematics and Ecology. 2005;33(7):729-735.
doi:10.1016/j.bse.2004.12.010 .
Jankovic, T, Krstić, Dijana, Aljančić, Ivana, Savikin-Fodulovic, K, Menković, N., Vajs, Vlatka, Milosavljevic, S, "Xanthones and C-glucosides from the aerial parts of four species of Gentianella from Serbia and Montenegro" in Biochemical Systematics and Ecology, 33, no. 7 (2005):729-735,
https://doi.org/10.1016/j.bse.2004.12.010 . .
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Phytochemical investigation of Gentiana dinarica

Krstić, Dijana; Jankovic, T; Aljančić, Ivana; Savikin-Fodulovic, K; Menković, N.; Milosavljevic, S

(Pergamon-Elsevier Science Ltd, Oxford, 2004)

TY  - JOUR
AU  - Krstić, Dijana
AU  - Jankovic, T
AU  - Aljančić, Ivana
AU  - Savikin-Fodulovic, K
AU  - Menković, N.
AU  - Milosavljevic, S
PY  - 2004
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/657
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Biochemical Systematics and Ecology
T1  - Phytochemical investigation of Gentiana dinarica
VL  - 32
IS  - 10
SP  - 937
EP  - 941
DO  - 10.1016/j.bse.2004.03.007
ER  - 
@article{
author = "Krstić, Dijana and Jankovic, T and Aljančić, Ivana and Savikin-Fodulovic, K and Menković, N. and Milosavljevic, S",
year = "2004",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Biochemical Systematics and Ecology",
title = "Phytochemical investigation of Gentiana dinarica",
volume = "32",
number = "10",
pages = "937-941",
doi = "10.1016/j.bse.2004.03.007"
}
Krstić, D., Jankovic, T., Aljančić, I., Savikin-Fodulovic, K., Menković, N.,& Milosavljevic, S.. (2004). Phytochemical investigation of Gentiana dinarica. in Biochemical Systematics and Ecology
Pergamon-Elsevier Science Ltd, Oxford., 32(10), 937-941.
https://doi.org/10.1016/j.bse.2004.03.007
Krstić D, Jankovic T, Aljančić I, Savikin-Fodulovic K, Menković N, Milosavljevic S. Phytochemical investigation of Gentiana dinarica. in Biochemical Systematics and Ecology. 2004;32(10):937-941.
doi:10.1016/j.bse.2004.03.007 .
Krstić, Dijana, Jankovic, T, Aljančić, Ivana, Savikin-Fodulovic, K, Menković, N., Milosavljevic, S, "Phytochemical investigation of Gentiana dinarica" in Biochemical Systematics and Ecology, 32, no. 10 (2004):937-941,
https://doi.org/10.1016/j.bse.2004.03.007 . .
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Chemical aspects of the influence of cobalt ions on ATPase activity

Vujisić, Ljubica; Krstić, Danijela; Vucetic, J

(Serbian Chemical Soc, Belgrade, 2000)

TY  - JOUR
AU  - Vujisić, Ljubica
AU  - Krstić, Danijela
AU  - Vucetic, J
PY  - 2000
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/438
AB  - The influence of Co2+ ions on the activities of Na+/K+-ATPase and Mg2+-ATPase, enzymes from rat brain synaptic plasma membrane, was studied. The aim of this study was to investigate the inhibition of both ATPases activities by exposure to cobalt ions as a function of experimentally added CoSO4. The "free" Co2+ concentrations in the reaction mixture were also calculated and discussed. CoSO4 induced a dose-dependent inhibition of both enzymes. The IC50 values of Co2+, as calculated from the experimental curves, were 168 mu M for Na+/K+-ATPase and 262 mu M for Mg2+-ATPase, and for the recalculated free Co2+ concentration 75.4 mu M for Na+/K+-ATPase and 136 mu M for Mg2+-ATPase. The obtained linear Dixon's plot for Na+/K+-ATPase implies equilibrium binding of cobalt with inhibitory sites on the enzyme. The kinetic parameters for both enzymes in presence and absence of CoSO4 were calculated from the experimental data. The results of the kinetic analysis show that inhibition of Na+/K+-ATPase induced by CoSO4 is non-competitive, and for Mg2+-ATPAse that there are two sites of different sensitivities or two different enzymes.
AB  - Ispitan je uticaj Co2+ jona na aktivnost Na+/K+ -ATPaze i Mg2+ -ATP-aze, enzima sinaptozomalne membrane mozga pacova. Cilj rada je bio da se ispita inhibicija aktivnosti oba enzima izazvana izlaganjem jonima kobalta kao funkcija eksperimentalno dodatog CoSO4. Takođe je izračunata i diskutovana "slobodna" koncentracija Co2+ u reakcionoj smeši. Utvrđeno je da kobalt inhibira enzime u koncentraciono zavisnom smislu. Vrednosti IC50 izračunate iz eksperimentalnih krivih su: 168 μM za Na+/K+ -ATP-azu i 136 μM za Mg2+ -ATP-azu. Linearan Dixon-ov plot za Na+/K+ -ATP-azu ukazuje na ravnotežno vezivanje kobalta. Izračunati su kinetički parametri oba enzima u prisustvu i odsustvu CoSO4. Inhibicija Na+/K+-ATP-aze izazvana CoSO4 je nekompetitivna, dok Mg2+ -ATP-aza ima dva mesta vezivanja različitog afiniteta ili pak dva različita enzima.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Chemical aspects of the influence of cobalt ions on ATPase activity
T1  - Hemijski aspekt uticaja jona kobalta na aktivnost ATP-aza
VL  - 65
IS  - 7
SP  - 507
EP  - 515
DO  - 10.2298/JSC0007507V
ER  - 
@article{
author = "Vujisić, Ljubica and Krstić, Danijela and Vucetic, J",
year = "2000",
abstract = "The influence of Co2+ ions on the activities of Na+/K+-ATPase and Mg2+-ATPase, enzymes from rat brain synaptic plasma membrane, was studied. The aim of this study was to investigate the inhibition of both ATPases activities by exposure to cobalt ions as a function of experimentally added CoSO4. The "free" Co2+ concentrations in the reaction mixture were also calculated and discussed. CoSO4 induced a dose-dependent inhibition of both enzymes. The IC50 values of Co2+, as calculated from the experimental curves, were 168 mu M for Na+/K+-ATPase and 262 mu M for Mg2+-ATPase, and for the recalculated free Co2+ concentration 75.4 mu M for Na+/K+-ATPase and 136 mu M for Mg2+-ATPase. The obtained linear Dixon's plot for Na+/K+-ATPase implies equilibrium binding of cobalt with inhibitory sites on the enzyme. The kinetic parameters for both enzymes in presence and absence of CoSO4 were calculated from the experimental data. The results of the kinetic analysis show that inhibition of Na+/K+-ATPase induced by CoSO4 is non-competitive, and for Mg2+-ATPAse that there are two sites of different sensitivities or two different enzymes., Ispitan je uticaj Co2+ jona na aktivnost Na+/K+ -ATPaze i Mg2+ -ATP-aze, enzima sinaptozomalne membrane mozga pacova. Cilj rada je bio da se ispita inhibicija aktivnosti oba enzima izazvana izlaganjem jonima kobalta kao funkcija eksperimentalno dodatog CoSO4. Takođe je izračunata i diskutovana "slobodna" koncentracija Co2+ u reakcionoj smeši. Utvrđeno je da kobalt inhibira enzime u koncentraciono zavisnom smislu. Vrednosti IC50 izračunate iz eksperimentalnih krivih su: 168 μM za Na+/K+ -ATP-azu i 136 μM za Mg2+ -ATP-azu. Linearan Dixon-ov plot za Na+/K+ -ATP-azu ukazuje na ravnotežno vezivanje kobalta. Izračunati su kinetički parametri oba enzima u prisustvu i odsustvu CoSO4. Inhibicija Na+/K+-ATP-aze izazvana CoSO4 je nekompetitivna, dok Mg2+ -ATP-aza ima dva mesta vezivanja različitog afiniteta ili pak dva različita enzima.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Chemical aspects of the influence of cobalt ions on ATPase activity, Hemijski aspekt uticaja jona kobalta na aktivnost ATP-aza",
volume = "65",
number = "7",
pages = "507-515",
doi = "10.2298/JSC0007507V"
}
Vujisić, L., Krstić, D.,& Vucetic, J.. (2000). Chemical aspects of the influence of cobalt ions on ATPase activity. in Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 65(7), 507-515.
https://doi.org/10.2298/JSC0007507V
Vujisić L, Krstić D, Vucetic J. Chemical aspects of the influence of cobalt ions on ATPase activity. in Journal of the Serbian Chemical Society. 2000;65(7):507-515.
doi:10.2298/JSC0007507V .
Vujisić, Ljubica, Krstić, Danijela, Vucetic, J, "Chemical aspects of the influence of cobalt ions on ATPase activity" in Journal of the Serbian Chemical Society, 65, no. 7 (2000):507-515,
https://doi.org/10.2298/JSC0007507V . .
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