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The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems / V. A. Kratasyuk [et al.] // Chemosphere. - 2001. - Vol. 42, Is. 8. - P909-915, DOI 10.1016/S0045-6535(00)00177-6 . - ISSN 0045-6535
Кл.слова (ненормированные):
Alcohol dehydrogenase -- Bacterial luciferase -- Bioluminescence -- Blooming -- Pollution -- Trypsin -- Water toxicity -- alcohol dehydrogenase -- benzoquinone -- luciferase -- trypsin -- aquatic ecosystem -- bioluminescence -- water quality -- article -- bacterium culture -- bioluminescence -- blue green alga -- ecosystem -- pond -- seasonal variation -- water pollution -- water quality -- Benzoquinones -- Biological Assay -- Cyanobacteria -- Ecosystem -- Environmental Monitoring -- Eutrophication -- FMN Reductase -- Indicators and Reagents -- Luminescent Measurements -- NADH, NADPH Oxidoreductases -- Water Pollutants -- Russian Federation -- algae -- Bacteria (microorganisms) -- Chlorophyta -- Cyanobacteria -- uncultured cyanobacterium
Аннотация: A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies. В© 2001 Elsevier Science Ltd.

Scopus
Держатели документа:
Krasnoyarsk State University, pr. Svobodnii 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Mira av., 88, Krasnoyarsk, 660049, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Esimbekova, E.N.; Gladyshev, M.I.; Khromichek, E.B.; Kuznetsov, A.M.; Ivanova, E.A.

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EFFICIENCY OF THE FUNCTIONING OF THE BIENZYMATIC SYSTEM NADH-FMN OXIDOREDUCTASE LUCIFERASE OF LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV, N. S. RODIONOVA, P. I. BELOBROV // Biochem.-Moscow. - 1985. - Vol. 50, Is. 3. - P338-342. - Cited References: 13 . - 5. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; RODIONOVA, N.S.; BELOBROV, P.I.

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2-ENZYME NADH-FMN-OXIDOREDUCTASE-LUCIFERASE SYSTEM FROM LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV [et al.] // Biochem.-Moscow. - 1984. - Vol. 49, Is. 4. - P593-603. - Cited References: 24 . - 11. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

Держатели документа:
LV KIRENSKII PHYS INST,KRASNOYARSK,USSR : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; KRATASYUK, G.A.; RODIONOVA, N.S.; FISH, A.M.; BELOBROV, P.I.

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Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

Scopus
Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Lee, J.

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А.с. 1027615 СССР, МКИ G 01 N 33/48.

Способ определения активности протеаз [Текст] / В. Н. Петушков [и др.] ; Ин-т физ. им. Л. В. Киренского. - № 3311598/28-13 ; Заявл. 30.06.19811983. -

ГРНТИ

34.15.19

РУБ 343.15.19
Рубрики:
ПРОТЕАЗЫ
   ТРИПСИН КФ 3
   1
   АКТИВНОСТЬ
   ОПРЕДЕЛЕНИЕ
   МЕТОД
   БИОЛЮМИНЕСЦЕНЦИЯ
   NADH:FMN-ОКСИДОРЕДУКТАЗА КФ 1
   ЛЮЦИФЕРАЗА
   ПРИМЕНЕНИЕ
   ФЕРМЕНТНАЯ КОМПОЗИЦИЯ
   TRYPSIN EC
   ACTIVITY DETERMINATION
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Петушков, Валентин Николаевич; Кратасюк, Г. А.; Фиш, А. М.; Гительзон, Иосиф Исаевич; Ин-т физ. им. Л. В. Киренского
Свободных экз. нет
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^a314.27.17^2VINITI
П 31

Петушков, В. Н.
Изучение эффективности работы биферментной системы NADH: FMN-оксидоредуктаза-люцифераза светящихся бактерий [Текст] : научное издание / В. Н. Петушков, Н. С. Родионова, П. И. Белобров // Биохимия. - 1985. - Т. 50, N 3. - С. 401-405 . - ISSN 0320-9725

ГРНТИ

31.27.17

РУБ 314.27.17
Рубрики:
НАДН:ФМН-ОКСИДОРЕДУКТАЗА-ЛЮЦИФЕРАЗА
   МЕХАНИЗМ РАБОТЫ
   БАКТЕРИИ
   СВЕТЯЩИЕСЯ
   NADH:FMN-OXIDOREDUCTASE-LUCIFERASE
   LUMINESCENT BACTERIA
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Родионова, Н.С.; Белобров, П.И.

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Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase / A. Bezrukikh [et al.] // . - 2014, DOI 10.1007/s00216-014-7987-1 . - ISSN 1618-2642
Кл.слова (ненормированные):
Bacterial luciferase -- Bioluminescence -- Gelatin -- NADH:FMN-oxidoreductase -- Stabilization of enzymes -- Starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 °C and 25 °C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 °C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions. © 2014 Springer-Verlag Berlin Heidelberg.

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A.; Esimbekova, E.; Nemtseva, E.; Kratasyuk, V.; Shimomura, O.

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Comparison of chronic low-dose effects of alpha- and beta-emitting radionuclides on marine bacteria / M. A. Selivanova [et al.] // Cent. Eur. J. Biol. - 2014. - Vol. 9, Is. 10. - P951-959, DOI 10.2478/s11535-014-0331-0 . - ISSN 1644-3632
Кл.слова (ненормированные):
Am-241 -- Hormesis -- Luminous bacteria -- Peroxides -- Radiotoxicity -- Tritium
Аннотация: Effects of Americium-241 (241Am), alpha-emitting radionuclide of high specific radioactivity, and tritium (3H), beta-emitting radionuclide, on luminous bacteria Photobacterium phosphoreum were compared. Bioluminescence intensity served as a marker of bacterial physiological activity. Three successive stages in the bioluminescence response to 241Am and 3H were found under conditions of lowdose irradiation: (1) absence of effects, (2) activation, and (3) inhibition. They were interpreted in terms of bacterial response to stressfactor as stress recognition, adaptive response/syndrome, and suppression of physiological function (i.e. radiation toxicity). Times of bioluminescence activation (TBA) and inhibition (TBI) were suggested as parameters to characterize hormesis and toxic stages in a course of chronic low-dose irradiation of the microorganisms. Values of TBA and TBI of 241Am were shorter than those of 3H, revealing higher impact of alpha-irradiation (as compared to beta-irradiation) under comparable radiation doses. Increases of peroxide concentration and NADH oxidation rates in 241Am aquatic solutions were demonstrated; these were not found in tritiated water. The results reveal a biological role of reactive oxygen species generated in water solutions as secondary products of the radioactive decay. The study provides a scientific basis for elaboration of bioluminescence-based assay to monitor radiotoxicity of alpha- and beta-emitting radionuclides in aquatic solutions. © 2014 Versita Warsaw and Springer-Verlag Wien.

Scopus
Держатели документа:
Institute of Biophysics SB RAS, 660036 Krasnoyarsk, Russian Federation
Siberian Federal University, 660041 Krasnoyarsk, Russian Federation
Siberian State Technological University, Lesosibirsk, Krasnoyarsk region, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Selivanova, M.A.; Rozhko, T.V.; Devyatlovskaya, A.N.; Kudryasheva, N.S.

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Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase [Text] / A. . Bezrukikh [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5743-5747, DOI 10.1007/s00216-014-7987-1. - Cited References: 14. - The work was supported by the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11.G34.31.0058), the Russian Academy of Sciences (program "Molecular and Cell Biology", grant no. 6.8), and the state contract between the Ministry of Education and Science and Siberian Federal University, no. 1762. . - ISSN 1618-2642. - ISSN 1618-2650

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
IMMOBILIZATION
CHEMISTRY
Кл.слова (ненормированные):
Bacterial luciferase -- NADH:FMN-oxidoreductase -- Bioluminescence -- Stabilization of enzymes -- Gelatin -- Starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 A degrees C and 25 A degrees C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 A degrees C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions.

WOS
Держатели документа:
[Bezrukikh, Anna
Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A...; Esimbekova, E...; Nemtseva, E...; Kratasyuk, V...; Shimomura, O...; Government of Russian Federation [11.G34.31.0058]; Russian Academy of Sciences [6.8]; Ministry of Education and Science [1762]; Siberian Federal University [1762]

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10.

EFFICIENCY OF THE FUNCTIONING OF THE BIENZYMATIC SYSTEM NADH-FMN OXIDOREDUCTASE LUCIFERASE OF LUMINESCENT BACTERIA [Text] / V. N. PETUSHKOV, N. S. RODIONOVA, P. I. BELOBROV // Biochem.-Moscow. - 1985. - Vol. 50, Is. 3. - P. 338-342. - Cited References: 13 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.; RODIONOVA, N.S.; BELOBROV, P.I.

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11.

A GEL MODEL FOR THE FUNCTIONING OF LUCIFERASE IN THE CELL [Text] / V. A. KRATASYUK, V. V. ABAKUMOVA, N. B. KIM // Biochem.-Moscow. - 1994. - Vol. 59, Is. 7. - P. 761-765. - Cited References: 11 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENT
Кл.слова (ненормированные):
BIOLUMINESCENCE -- LUCIFERASE -- NADH, FMN-OXIDOREDUCTASE -- IMMOBILIZATION
Аннотация: A gel model for the functioning of luciferase in cells has been constructed using bacterial NADH:FMN-oxidoreductase and luciferase immobilized in starch gel disks. The characteristics of the immobilized luciferase depend on the duration of drying, the amount and concentration of the gel, the nature of the support used for drying, and the properties of the initial enzyme preparation. Functionally important enzyme groups remain intact in the immobilized preparation, and luciferase retains its high specificity with respect to aldehydes. The gel microenvironment appears to be optimal for luciferase, judging from its high activity and increased stability. Conditions allowing repeated use of the preparation have been found. The approach permits co-immobilization of luciferase with other enzymes and their substrates. The error in bioluminescence measurements using the disks is 5-10%. A procedure for stabilization of the immobilized luciferase during repeated use has been devised.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
KRATASYUK, V.A.; ABAKUMOVA, V.V.; KIM, N.B.

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12.

Metallic salts action on bacterial bioluminescent systems of different complexity [Текст] / N. S. Kudryasheva [и др.] // Biofizika. - 1996. - Vol. 41, Is. 6. - P. 1264-1269. - Cited References: 12 . - ISSN 0006-3029

РУБ Biophysics

Аннотация: Action of metallic salts on the bacterial bioluminescent systems (1 - water-soluble coupled system luciferase - NADH:FMN-oxydoreductase; 2 - immobilized in starch gel coupled system luciferase - NADH:FMN-oxydoreductase; 3 - intact bacteria) has been studied. The action parameters have been calculated. The effects have been shown to depend on nature of cations but not anions. Electronic structure of cations (nature of external orbitals, charge, radii) has been taken into account. Cations with similar electronic shells nature affect on the row of the bioluminescent systems mentioned above in a similar way. Differences in effects have been explained with diffusion rate, cellular shell and respiration of bacteria.

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Zuzikova, E.V.; Gutnyk, T.V.; Kuznetsov, A.M.

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13.

A biological luciferase test for the bioluminescent assay of wheat grain infection with Fusarium [Text] / V. A. Kratasyuk [et al.] // Appl. Biochem. Microbiol. - 1998. - Vol. 34, Is. 6. - P. 622-624. - Cited References: 7 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The extent of inhibition of the bioluminescence reaction by wheat grain extracts was studied as a function of the scabby kernel content in wheat. The NADH : flavine mononucleotide oxidoreductase-luciferase bienzyme bioluminescence system was found to be the most sensitive to mycotoxins produced by fungi of the genus Fusarium. A biological luciferase test was developed for monitoring wheat grain infection with Fusarium.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
All Russia Res Inst Grain & Grain Prod, Moscow 127434, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Egorova, O.I.; Esimbekova, E.N.; Kudryashova, N.S.; Orlova, N.Y.; L'vova, L.S.

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14.

Effect of Fusarium mycotoxins an a bacterial bioluminescence system in vitro [Text] / V. A. Kratasyuk [et al.] // Appl. Biochem. Microbiol. - 1998. - Vol. 34, Is. 2. - P. 190-192. - Cited References: 7 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The effects of the mycotoxins produced by fungi of the genus Fusarium on the NADH : Ravine mononucleotide oxidoreductase-luciferase bacterial bioluminescence system was studied. The sensitivity of the bioluminescence system to mycotoxins decreases in the following order: zearalenone, deoxynivalenol, toxin T-2, and diacetoxiscripenol. These results allow the development of a luciferase bioluminescence test system for rapid control of grain infection with Fusarium.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
All Russian Res Inst Grain & Grain Prod, Moscow 127434, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660062, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; L'vova, L.S.; Egorova, O.I.; Kudryasheva, N.S.; Orlova, N.Y.; Bytev, V.O.

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15.

Bioluminescent water quality monitoring of salt lake Shira [Text] / V. A. Kratasyuk, E. V. Vetrova, N. S. Kudryasheva // Luminescence. - 1999. - Vol. 14: 10th International Symposium on Bioluminescence and Chemiluminescence (1998, BOLOGNA, ITALY), Is. 4. - P. 193-195, DOI 10.1002/(SICI)1522-7243(199907/08)14:4193::AID-BIO5283.3.CO;2-J. - Cited References: 9 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bioluminescence -- biotest -- ecological monitoring -- salt lake
Аннотация: The coupled bioluminescent enzyme system luciferase-NADH:FMN-oxidoreductase was used as a biotest in ecological monitoring of the health resort salt lake Shira (South Siberia, Russia). The technique was adapted to saltwater conditions. Bioluminescence kinetic parameters sensitive to pollutants were determined. Conditions for the use of bacterial bioluminescence biotests in salty environmental media were established. Copyright (C) 1999 John Wiley & Sons, Ltd.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, SB, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Vetrova, E.V.; Kudryasheva, N.S.

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16.

Mechanism of action of metal salts on bacterial bioluminescent system in vitro [Текст] / N. S. Kydryasheva, E. V. Zuzikova, T. V. Gutnik // Biofizika. - 1999. - Vol. 44, Is. 2. - P. 244-250. - Cited References: 21 . - ISSN 0006-3029

РУБ Biophysics

Кл.слова (ненормированные):
bacterial bioluminescent system -- metal salts, mechanism of action
Аннотация: The action of met al salts on the luciferase-NADH: FMN-oxydoheductase bacterial luminescent system in vitro was studied. The effect is shown to depend on the nature of cations rather than anions, The type of the effect (activation, inhibition, and absence of the effect) is determined by the structure of the; cation, the nature and occupancy of its external orbitals, and charge. The results were interpreted on the basis of the hypothesis that upper electron excited states of the emitter are involved in the bioluminescence process. Based on thermodynamic calculations, the type of the effect was related to the energetic characteristics of the cation, Presumably, the mechanism of action of cations is determined by their involvement in the formation and deactivation of electron excited states in the bioluminescence process.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kydryasheva, N.S.; Zuzikova, E.V.; Gutnik, T.V.

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17.

The influence of quinones and phenols on the triple NAD(H)-dependent enzyme systems [Text] / N. S. Kudryasheva [et al.] // Chemosphere. - 1999. - Vol. 38, Is. 4. - P. 751-758, DOI 10.1016/S0045-6535(98)00218-5. - Cited References: 7 . - ISSN 0045-6535

РУБ Environmental Sciences

Аннотация: Kinetics of the triple bioluminescent enzyme system: alcohol dehydrogenase - NADH:FMN-oxidoreductase - luciferase in the presence of quinones and phenols has been studied. The correspondence between the bioluminescent kinetic parameters, redox potentials and concentrations of the quinones and phenols has been estimated. The substances have been shown to change bioluminescent kinetics through moving off the NAD(+)/NADH balance in the enzyme processes. This system is proposed to be used as enzymatic biotest in ecological monitoring. (C) 1998 Elsevier Science Ltd. All rights reserved.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
Irkutsk State Univ, Biol Res Inst, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Kudinova, I.Y.; Esimbekova, E.N.; Kratasyuk, V.A.; Stom, D.I.

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18.

Effects of quinones on NADH-dependent enzymatic bioluminescent systems [Text] / N. S. Kudryasheva [et al.] // Appl. Biochem. Microbiol. - 2000. - Vol. 36, Is. 4. - P. 409-413, DOI 10.1007/BF02738052. - Cited References: 13 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The effects of a number of quinones on the bioluminescence characteristics of a three-component enzymatic system containing alcohol dehydrogenase, bacterial luciferase, and NADH-FMN oxidoreductase were studied to find the most sensitive kinetic parameters of the system intended to be used in biological testing. Both direct and back reactions catalyzed by alcohol dehydrogenase were studied in the presence and in the absence of quinones. The kinetic parameters of the bioluminescent system were found to depend on the redox potentials and concentrations of quinones. The quinone-induced effects were shown to be associated with changes in the NAD(+)/NADH ratio in the chain of NADH-dependent enzymes, The three-enzyme system based on alcohol dehydrogenase is suggested as a bioluminescence test for ecological monitoring of waste water.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
Irkutsk State Univ, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Esimbekova, E.N.; Kudinova, I.Y.; Kratasyuk, V.A.; Stom, D.I.

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19.

Estimation of energy of the upper electron-excited states of the bacterial bioluminescent emitter [Text] / N. S. Kudryasheva [et al.] // J. Photochem. Photobiol. B-Biol. - 2002. - Vol. 68, Is. 02.03.2013. - P. 88-92, DOI 10.1016/S1011-1344(02)00360-3. - Cited References: 25 . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MECHANISM
Кл.слова (ненормированные):
bioluminescence -- electron-excited states -- energy transfer
Аннотация: The hypothesis of activity of the upper electron-excited states of the bacterial bioluminescent emitter was verified using dye molecules as foreign energy acceptors. Six compounds were selected having fluorescent state energies ranging from 25 700 to 32 000 cm(-1) (anthracene, pyrene, 1.4-bis(5-phenyloxasol-2-yl)benzene (POPOP), p-bis(o-methylstyryl)benzene (MSB), 2-methoxy-naphtalene, p-terphenyl), exceeding that of the bioluminescent emitter (22 000 cm(-1)). Their absorption spectra do not overlap with the bioluminescence spectrum; the trivial light absorption and the intermolecular resonance S-S energy transfer were excluded. Bacterial bioluminescent spectra of the coupled enzyme system NADH:FMN-oxidoreductase-luciferase in the presence of MSB were presented as an example. The weak sensitized fluorescence of MSB was registered. The results obtained have confirmed the activity of the energetic precursor in the bacterial bioluminescence. Its energy can be located in the interval of 26 000-27 000 cm(-1). (C) 2002 Published by Elsevier Science B.V.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Akademgorodok 660036, Krasnoyarsk, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660049, Russia
Wageningen Univ, Microspect Ctr, Dept Biomol Sci, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Nemtseva, E.V.; Sizykh, A.G.; Kratasyuk, V.A.; Visser, AJWG

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20.

Bioluminescence assays: Effects of quinones and phenols [Text] / N. . Kudryasheva [et al.] // Ecotox. Environ. Safe. - 2002. - Vol. 53, Is. 2. - P. 221-225, DOI 10.1006/eesa.2002.2214. - Cited References: 18 . - ISSN 0147-6513

РУБ Environmental Sciences + Toxicology

Кл.слова (ненормированные):
bioluminescence assays -- quinones -- phenols
Аннотация: The influence of a series of quinones and phenols on bacterial bioluminescence systems was investigated. Three bioluminescence systems used in ecological monitoring were compared: (1) water-soluble; (2) immobilized in starch gel coupled enzyme systems: NADH:FMN-oxidoreductase-luciferase; (3) luminescent bacteria. Bioluminescence inhibition constants of quinones and phenols and bioluminescence induction periods were compared. These kinetic parameters are proportional to quinone concentrations and depend on the quinone redox potential. Different effects of the substances are related to structure and properties of the bioluminescence systems. The set of bioluminescence assays for quinones and phenols monitoring should include two bioluminescence systems: 1 (or 2) and 3. (C) 2002 Elsevier Science (USA).

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
Irkutsk State Univ, Biol Res Inst, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N...; Vetrova, E...; Kuznetsov, A...; Kratasyuk, V...; Stom, D...

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