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Bacterial bioluminescence and bioluminescent analysis / V. A. Kratasyuk, I. I. Gitel'zon // Biophysics. - 1982. - Vol. 27, Is. 6. - P977-995 . - ISSN 0006-3509
Аннотация: The principles of bioluminescent analysis and the current methods of quantitatively analysing different substances based on the use of bioluminescence of luminous bacteria and enzyme-substrate systems isolated from them are considered. The prospects of using bioluminescent methods in science, medicine and industry are discussed. В© 1983.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, U.S.S.R. Academy of Sciences, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Gitel'zon, I.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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^a343.15.19^2VINITI
П 31

Петушков, В. Н.
Биолюминесцентный анализ НАДН-зависимых дегидрогеназ [Текст] : научное издание / В. Н. Петушков, Л. П. Шефер, Н. С. Родионова // Получ. и применение биокатализаторов в нар. х-ве и мед. Тез. докл. 5 Всес. симп. по инж. энзимол., Кобулети, май, 1985. Т. 1. - Олайне, 1985. - С. 168

ГРНТИ

34.15.19

РУБ 343.15.19
Рубрики:
НАДНДЕГИДРОГЕНАЗА
   ОПРЕДЕЛЕНИЕ
   БИОЛЮМИНЕСЦЕНТНЫЙ МЕТОД
   НАДН-ФМНОКСИДОРЕДУКТАЗА
   ЛЮЦИФЕРАЗА
   БИОЛЮМИНЕСЦЕНТНАЯ СИСТЕМА
   ENZYME SYSTEMS
   ANALYTICAL USES
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Шефер, Л.П.; Родионова, Н.С.

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Obtaining bacterial luciferase for bioluminescent analysis / V. S. Bondar [и др.] // Prikladnaya Biokhimiya i Mikrobiologiya. - 1988. - Vol. 24, Is. 6. - С. 745-753 . - ISSN 0555-1099
Кл.слова (ненормированные):
luciferase -- enzyme isolation -- enzyme subunit structure -- molecular weight -- nonhuman -- photobacterium leiognathi

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch of the USSR Academy of Sciences, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bondar, V.S.; Vysotsky, E.S.; Zavoruev, V.V.; Mezhevikin, V.V.; Raibekas, A.A.

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EFFECT OF TEMPERATURE ON ACTIVITY AND STABILITY OF OBELIN [Text] / V. S. BONDAR [et al.] // Biochem.-Moscow. - 1992. - Vol. 57, Is. 7. - P717-724. - Cited References: 15 . - 8. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CA-2+
PHOTOPROTEINS
INDICATORS
Кл.слова (ненормированные):
PHOTOPROTEINS -- OBELIN -- ACTIVATION ENERGY -- THERMOINACTIVATION -- THERMOSTABILITY
Аннотация: The temperature dependence of bioluminescent activity of the Ca2+-activated photoprotein obelin from the hydroid polyp Obelia longissima and thermoinactivation of this protein at different concentrations of (NH4)2SO4 have been studied. The maximal intensity of luminescence of obelin was observed at 4-15-degrees-C. The activity of the photoprotein is completely stable to storage for 3 days at room temperature. Increasing the temperature to 40-degrees-C resulted in a 25-30% loss of enzyme activity in 1 h. The presence of ammonium sulfate during heating stabilizes the activity of obelin. Two breaks, at 11 +/- 3-degrees-C and 47 +/- 3-degrees-C, are observed in the Arrhenius plot of the first-order rate constant of the luminescence decay. The bioluminescent curves of obelin are biphasic in the temperature range 10-40-degrees-C. It is assumed that obelin may exist in two kinetically distinct conformers (active and inactive) whose ratio is temperature dependent.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; TROFIMOV, K.P.; SANDALOV, T.P.; VYSOTSKII, E.S.

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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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LOCALIZATION OF ACTIVE-SITE OF ENZYME, BACTERIAL LUCIFERASE, USING 2-QUANTUM AFFINITY MODIFICATION [Текст] / L. Z. BENIMETSKAYA [и др.] // Dokl. Akad. Nauk. - 1994. - Vol. 336, Is. 1. - С. 114-117. - Cited References: 10 . - ISSN 0869-5652

РУБ Multidisciplinary Sciences

Держатели документа:
RUSSIAN ACAD SCI,SIBERIAN DIV,INST BIOPHYS,KRASNOYARSK,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
BENIMETSKAYA, L.Z.; KOZIONOV, A.L.; NOVOZHILOV, S.Y.; PETUSHKOV, V.N.; RODIONOVA, N.S.; SHTOKMAN, M.I.

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Comparative study of temperature effects on bacterial luciferases [Text] / N. A. Tyulkova, T. P. Sandalova // Biochem.-Moscow. - 1996. - Vol. 61, Is. 2. - P. 205-214. - Cited References: 23 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENCE
Кл.слова (ненормированные):
bacterial luciferase -- temperature -- activation energy
Аннотация: Effects of temperature on bioluminescent patterns of luciferases from luminescent bacteria Vibrio harveyi, Vibrio fischeri, Photobacterium leiognathi, and Photobacterium phosphoreum were studied. The highest luminescence level was observed at 15-25 degrees C for the luciferase from P. phosphoreum, at 20-30 degrees C for the V. fischeri and P. leiognathi enzymes, and at 30-37 degrees C for the enzyme from V. harveyi. All the luciferases were significantly stabilized at increased salt concentrations, at low pH values, or in the presence of dithiothreitol (DTT) and EDTA. The addition of DTT and EDTA affected the reversible stage of enzyme inactivation, while salts reduced the rate of the irreversible stage. A peak corresponding to aggregated protein was detected by gel chromatography of irreversibly inactivated luciferase. Activation energies were calculated for each luciferase in bioluminescent reactions with decanal, dodecanal, tetradecanal, and without aldehydes. The activation energy of the reaction with tetradecanal was much lower than those with the other aldehydes. The temperature dependence of the lifetime of the long-lived reaction intermediate showed that in the 10-30 degrees C interval all the luciferases, except for the enzyme from V. harveyi, have only one active form.

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

Доп.точки доступа:
Tyulkova, N.A.; Sandalova, T.P.

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Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (antenna) proteins: Bioluminescence effects of the aliphatic additive / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- anisotropy -- antenna -- article -- bioluminescence -- complex formation -- energy transfer -- enzyme active site -- enzyme kinetics -- nonhuman -- priority journal -- protein protein interaction -- spectroscopy -- vibrionaceae -- Bacterial Proteins -- Carrier Proteins -- Cloning, Molecular -- Dithionite -- Flavin Mononucleotide -- Kinetics -- Luciferases -- Luminescent Measurements -- Luminescent Proteins -- Models, Structural -- Photobacterium -- Protein Binding -- Protein Conformation -- Recombinant Proteins -- Spectrophotometry -- Vibrio -- Bacteria (microorganisms) -- Photobacterium -- Photobacterium leiognathi -- Vibrio fischeri -- Vibrionaceae
Аннотация: The kinetics of the bacterial bioluminescence reaction is altered in the presence of the fluorescent (antenna) proteins, lumazine protein (LumP) from Photobacterium or the yellow fluorescence proteins (YFP) having FMN or Rf bound, from Vibrio fischeri strain Y1. Depending on reaction conditions, the bioluminescence intensity and its decay rate may be either enhanced or strongly quenched in the presence of the fluorescent proteins. These effects can be simply explained on the basis of the same protein-protein complex model that accounts for the bioluminescence spectral shifts induced by these fluorescent proteins. In such a complex, where the fluorophore evidently is in proximity to the luciferase active site, it is expected that the on off rate of certain aliphatic components of the reaction should be altered with a consequent shift in the equilibria among the luciferase intermediates, as recently elaborated in a kinetic scheme. These aliphatic components are the bioluminescence reaction substrate, tetradecanal or other long-chain aldehyde, its carboxylic acid product, or dodecanol used as a stabilizer of the luciferase peroxyflavin. No evidence can be found for the protein- protein interaction in the absence of the aliphatic component.

Scopus
Держатели документа:
Department of Biochemistry, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Acad. of Sci. of Russia, 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Ketelaars, M.; Gibson, B.G.; Lee, J.

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10.

Obelin as a carrier protein and reporter enzyme for in vitro synthesized small bioactive polypeptides: New approach to obtain sarcotoxin [Text] / B. A. Illarionov [et al.] ; ed.: JW Hastings, LJ Kricka, J Kricka, // BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS : JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT , 1996, WOODS HOLE, MA). - P. 435-438. - Cited References: 0 . - ISBN 0-471-97502-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Illarionov, B.A.; Matveev, S.V.; Bondar, V.S.; Skosyrev, V.A.; Alakhov, Y.B.; Hastings, JW \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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11.

Obelin as a carrier protein and reporter enzyme for in vitro synthesized small bioactive polypeptides: New approach to obtain sarcotoxin [Text] / B. A. Illarionov [et al.] ; ed.: JW Hastings, LJ Kricka, J Kricka, // BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS : JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT , 1996, WOODS HOLE, MA). - P435-438. - Cited References: 0 . - ISBN 0-471-97502-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Illarionov, B.A.; Matveev, S.V.; Bondar, V.S.; Skosyrev, V.A.; Alakhov, Y.B.; Hastings, JW \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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12.

Development of bioluminescent bioindicators for analysis of environmental pollution [Text] / N. . Kudryasheva [et al.] // Field Anal. Chem. Technol. - 1998. - Vol. 2, Is. 5. - P. 277-280, DOI 10.1002/(SICI)1520-6521(1998)2:5277::AID-FACT43.0.CO;2-P. - Cited References: 17 . - ISSN 1086-900X

РУБ Chemistry, Analytical + Environmental Sciences + Instruments & Instrumentation

Кл.слова (ненормированные):
biotest -- bioluminescence -- enzymes -- environmental monitoring
Аннотация: The influence of several suites of pollutants (metallic salts, quinones, and phenols) on bacterial bioluminescence in vivo and in vitro (five test systems) was investigated. The sensitivity of bioluminescence to the different pollutants was evaluated, and inhibition constants were measured. The data obtained were shown to correlate with the physical and chemical characteristics of the substances and the structure of the bioluminescent systems. It has been found that three bioluminescent tests (water-soluble enzyme systems, immobilized enzyme systems, and bioluminescent bacteria) show higher sensitivity to pollutants and cover all types of widespread contamination. These tests were chosen as a set of bioluminescent assays for the detection of pollutants. (C) 1998 John Wiley & Sons, Inc.

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

Доп.точки доступа:
Kudryasheva, N...; Kratasyuk, V...; Esimbekova, E...; Vetrova, E...; Nemtseva, E...; Kudinova, I...

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13.

Mechanisms of the effect of xenobiotics on bacterial bioluminescence [Text] / N. S. Kudryasheva // Luminescence. - 1999. - Vol. 14: 10th International Symposium on Bioluminescence and Chemiluminescence (1998, BOLOGNA, ITALY), Is. 4. - P. 199-200, DOI 10.1002/(SICI)1522-7243(199907/08)14:4199::AID-BIO5303.0.CO;2-X. - Cited References: 12 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
xenobiotics -- bioluminescence quenching -- energy -- electron and hydrogen transfer
Аннотация: The influence of xenobiotics on the bioluminescent enzyme system is considered in terms of molecular action on the primary physicochemical processes-energy, electron and hydrogen (e(-) + H+) transduction. Dyes, non-fluorescent chemically inert organic compounds, redox-active organic compounds and metallic salts were investigated. The influence of the different xenobiotics depends in a complex way on physicochemical characteristics of the xenobiotic molecules (spectral-luminescent characteristics, electron-acceptation energy and redox potential). 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:
Kudryasheva, N.S.

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14.

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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15.

High-resolution structures of scytalone dehydratase-inhibitor complexes crystallized at physiological pH [Text] / Z. . Wawrzak [et al.] // Proteins. - 1999. - Vol. 35, Is. 4. - P. 425-439, DOI 10.1002/(SICI)1097-0134(19990601)35:4425::AID-PROT63.0.CO;2-1. - Cited References: 33 . - ISSN 0887-3585

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
MAGNAPORTHE-GRISEA
   HEMAGGLUTININ
   GLYCOPROTEIN
   REFINEMENT
   MELANIN
   DISEASE
   SITE
Кл.слова (ненормированные):
structure-based design -- enzyme inhibitors -- X-ray crystallography -- fungicides -- melanin biosynthesis
Аннотация: Scytalone dehydratase is a molecular target of inhibitor design efforts aimed at preventing the fungal disease caused by Magnaporthe grisea. A method for cocrystallization of enzyme with inhibitors at neutral pH has produced several crystal structures of enzyme-inhibitor complexes at resolutions ranging from 1.5 to 2.2 Angstrom Four high resolution structures of different enzyme-inhibitor complexes are described. In contrast to the original X-ray structure of the enzyme, the four new structures have well-defined electron density for the loop region comprising residues 115-119 and a different conformation between residues 154 and 160. The structure of the enzyme complex with an aminoquinazoline inhibitor showed that the inhibitor is in a position to form a hydrogen bond with the amide of the Asn131 side chain and with two water molecules in a fashion similar to the salicylamide inhibitor in the original structure, thus confirming design principles. The aminoquinazoline structure also allows for a more confident assignment of donors and accepters in the hydrogen bonding network, The structures of the enzyme complexes with two dichlorocyclopropane carboxamide inhibitors showed the two chlorine atoms nearly in plane with the amide side chain of Asn131. The positions of Phe53 and Phe158 are significantly altered in the new structures in comparison to the two structures obtained from crystals grown at acidic pH, The multiple structures help define the mobility of active site amino acids critical for catalysis and inhibitor binding. Proteins 1999;35:425-439. (C) 1999 Wiley-Liss, Inc.

WOS
Держатели документа:
Dupont Co, Stine Haskell Res Ctr, Agr Prod, Newark, DE 19714 USA
Dupont Co, Expt Stn, Life Sci, Wilmington, DE USA
Karolinska Inst, Dept Med Biochem & Biophys, Stockholm, Sweden
Russian Acad Sci, Inst Biophys, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Wawrzak, Z...; Sandalova, T...; Steffens, J.J.; Basarab, G.S.; Lundqvist, T...; Lindqvist, Y...; Jordan, D.B.

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16.

Model of the active site of firefly luciferase [Text] / T. P. Sandalova, N. N. Ugarova // Biochem.-Moscow. - 1999. - Vol. 64, Is. 8. - P. 962-967. - Cited References: 20 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
ESCHERICHIA-COLI
   SEQUENCE
   CLONING
   ENZYME
   CDNA
   SUPERFAMILY
Кл.слова (ненормированные):
bioluminescence -- firefly luciferase -- ATP -- luciferin -- spatial structure -- active site -- enzyme-substrate complex
Аннотация: A model for the spatial structure of firefly luciferase-ATP-luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme-substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP-phenylalanine-synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Karolinska Inst, S-17177 Stockholm, Sweden
Moscow MV Lomonosov State Univ, Sch Chem, Moscow 119899, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Sandalova, T.P.; Ugarova, N.N.

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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.

WOS
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.

Investigation of culture heterogeneity of the hydrogen-oxidizing bacterium Alcaligenes eutrophus / G. N. Stasishina [et al.] // Microbiology. - 1999. - Vol. 68, Is. 2. - P164-170 . - ISSN 0026-2617
Кл.слова (ненормированные):
Dissociation -- Heterogeneity -- Hydrogen-oxidizing bacteria -- Ultrastructure of cells and colonies
Аннотация: Some morphological, physiological, and biochemical manifestations of heterogeneity in the population of the hydrogen-oxidizing bacterium Alcaligenes eutrophus Z1 were studied. The population dissociated into R and S variants differing in the size, appearance, and architectonics of colonies, cell ultrastructure, growth rate, enzyme activity, and chemical composition. Heterogeneity also manifested itself in different responses of cells to antibiotics, surfactants, and elevated temperature. В© 1999 MAHK "Hayka/Interperiodica".

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stasishina, G.N.; Mogil'naya, O.A.; Volova, T.G.; Guseinov, O.A.; Kalacheva, G.S.; Medvedeva, S.E.; Plotnikov, V.F.; Frank, L.A.

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19.

Practical enzymology course based on bioluminescence [Text] / V. A. Kratasyuk, I. Y. Kudinova // Luminescence. - 1999. - Vol. 14: 10th International Symposium on Bioluminescence and Chemiluminescence (1998, BOLOGNA, ITALY), Is. 4. - P. 189-192, DOI 10.1002/(SICI)1522-7243(199907/08)14:4189::AID-BIO5273.0.CO;2-E. - Cited References: 7 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
enzyme -- science education -- luciferase -- bioluminescence
Аннотация: We describe our experience with laboratory courses in enzymology based on the phenomenon of bioluminescence. The soluble and immobilized enzymes of luminous bacteria are used and the practical enzymological course consists of four main courses: (1) training in measuring the activities of soluble and immobilized enzymes; (2) the investigation of kinetic characteristics (kinetic constants) and enzyme-substrate and enzyme-inhibitor interactions in the bacterial bioluminescent reaction; (3) The testing of physico-chemical characteristics of enzymes (pH, temperature, ion strength, etc.); (4) the effect of inhibitors on enzymes. Training is possible in groups of about ten persons. Our practice work has been introduced in the biological, pedagogical and physical departments of Krasnoyarsk State University. Students of the pedagogical department have created a popular and interesting series of laboratory works for high school children aged 14-17 years. Copyright (C) 1999 John Wiley & Sons, Ltd.

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Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
Krasnoyarsk State Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V.A.; Kudinova, I.Y.

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20.

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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