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The effect of temperature on the growth kinetics of Candida tropicalis 29-10 continuously cultivated in the pH-stat at different growth-limiting conditions / A. V. Furyaeva, V. T. Shevchenko, N. S. Pechurkin // Prikladnaya Biokhimiya i Mikrobiologiya. - 1986. - Vol. 22, Is. 2. - С. 243-247 . - ISSN 0555-1099
Кл.слова (ненормированные):
candida tropicalis -- continuous culture -- fungus -- growth -- nonhuman -- ph -- temperature

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:
Furyaeva, A.V.; Shevchenko, V.T.; Pechurkin, N.S.

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EFFECT OF METABOLIC BOTTLENECK ORGANIZATION ON KINETICS OF ENZYMIC SUBSTRATE CONVERSION [Text] / R. P. TRENKENSHU // Mol. Biol. - 1988. - Vol. 22, Is. 6. - P. 1170-1177. - Cited References: 27 . - ISSN 0026-8933

РУБ Biochemistry & Molecular Biology

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
TRENKENSHU, R.P.

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SEASONAL DYNAMICS OF THE KINETICS OF NATURAL PHENOL DECONTAMINATION IN THE SYDIN BAY OF THE KRASNOYARSK WATER RESERVOIR [Текст] / M. I. GLADYSHEV, I. V. GRIBOVSKAIA, L. A. SHCHUR // DOKLADY AKADEMII NAUK SSSR. - 1990. - Vol. 313, Is. 6. - P. 1512-1514. - Cited References: 4 . - ISSN 0002-3264

РУБ Multidisciplinary Sciences

WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
GLADYSHEV, M.I.; GRIBOVSKAIA, I.V.; SHCHUR, L.A.

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CHEMILUMINESCENT ANALYSIS OF THE KINETICS OF REACTIVE OXYGEN SPECIES GENERATION BY WHOLE-BLOOD CELLS UNDER COMPENSATIVE EXFUSIONS [Текст] / K. I. PUKHOV [и др.] // DOKLADY AKADEMII NAUK SSSR. - 1991. - Vol. 316, Is. 1. - P. 247-251. - Cited References: 11 . - ISSN 0002-3264

РУБ Multidisciplinary Sciences
Рубрики:
HYDROGEN-PEROXIDE
NEUTROPHIL

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

Доп.точки доступа:
PUKHOV, K.I.; MAKARSKAYA, G.V.; YAKHNINA, Y.I.; PUKHOVA, Y.I.

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INACTIVATION OF BACTERIAL LUCIFERASES BY N-ETHYLMALEIMIDE [Text] / T. P. SANDALOVA, N. A. TYULKOVA // Biochem.-Moscow. - 1992. - Vol. 57, Is. 6. - P. 552-558. - Cited References: 21 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
AMINO-ACID SEQUENCE
   NUCLEOTIDE-SEQUENCE
   REACTIVE SULFHYDRYL
   PHOTOBACTERIUM-LEIOGNATHI
   VIBRIO-HARVEYI
   BIOLUMINESCENCE
   SUBUNIT
   REGION
   GENE
Кл.слова (ненормированные):
LUCIFERASE -- N-ETHYLMALEIMIDE
Аннотация: The kinetics of inactivation of luciferases from four species of luminescent bacteria by the thiol reagent N-ethylmaleimide were investigated The dependencies of inactivation on ionic strength differed among the enzymes. Increasing the molarity of the buffer increased the rate of inactivation of all luciferases except that of Vibrio harveyi. Modification of Photobacterium phosphoreum luciferase decreased the maximal intensity of bioluminescence, whereas modification of Photobacterium leiognathi and Vibrio fischeri luciferases in high ionic strength buffers decreased the maximal intensity of bioluminescence and changed the luminescence decay rate constant. High ionic strength apparently alters the conformational states of the luciferases.

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

Доп.точки доступа:
SANDALOVA, T.P.; TYULKOVA, N.A.

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DISAPPEARANCE OF PHENOL IN WATER SAMPLES TAKEN FROM THE YENISEI RIVER AND THE KRASNOYARSK RESERVOIR [Text] / M. I. GLADYSHEV, I. V. GRIBOVSKAYA, V. V. ADAMOVICH // Water Res. - 1993. - Vol. 27, Is. 6. - P1063-1070, DOI 10.1016/0043-1354(93)90071-O. - Cited References: 20 . - 8. - ISSN 0043-1354

РУБ Engineering, Environmental + Environmental Sciences + Water Resources
Рубрики:
ORGANIC-COMPOUNDS
   LAKE WATER
   MINERALIZATION
   BIODEGRADATION
   KINETICS
   MODELS
Кл.слова (ненормированные):
BIODEGRADATION -- PHENOL
Аннотация: Using experimental microecosystems the kinetics of phenol disappearance in river and reservoir water were investigated. In river water the disappearance kinetics could be described by A first-order equation, the same kinetics took place in reservoir water before and after the period of ''bloom'' of blue-green algae. During the ''bloom'', the phenol seemed to be mineralized by bacteria which grew at the expense of another compound, and the model of best fit was the model of exponential growth and low concentration of the test substrate. In the river, two sections differed according to the difference between the mean values of the specific disappearance rates. In the reservoir these rates were lower than those in the river. In general the specific disappearance rate values did not correlate with the values of initial bacterioplankton density, the concentrations of inorganic nutrients nor the chemical oxygen demand. Conclusions about the integral influence of ecosystems on the disappearance rates and dependence of self-purification kinetics on the type of aquatic ecosystem were made.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
GLADYSHEV, M.I.; GRIBOVSKAYA, I.V.; ADAMOVICH, V.V.

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Growth and luminescence of luminous bacteria promoted by agents of microbial origin. / E. K. Rodicheva [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P293-299 . - ISSN 0884-3996
Кл.слова (ненормированные):
amino acid -- carbohydrate -- folic acid -- luciferase -- nitrogen -- riboflavin -- article -- biosynthesis -- culture medium -- electron microscopy -- growth, development and aging -- kinetics -- luminescence -- metabolism -- Photobacterium -- physiology -- time -- ultrastructure -- Vibrio -- Amino Acids -- Carbohydrates -- Culture Media -- Folic Acid -- Kinetics -- Luciferase -- Luminescence -- Microscopy, Electron -- Nitrogen -- Photobacterium -- Riboflavin -- Time Factors -- Vibrio
Аннотация: The examination of four species of luminous bacteria Photobacterium leiognathi, Photobacterium phosphoreum, Vibrio fischeri and Vibrio harveyi has enabled us to reveal some nutrient medium components effecting growth, luminescence intensity and luciferase synthesis. These agents are nucleic components (nucleotides, nucleotides and amine bases), amino acids and vitamins, which are part of hydrolysates from the biomass of various lithotrophic microorganisms, hydrogen-oxidizing, iron-oxidizing and carboxydobacteria. The effect of promoting agents essentially alters the physiological state and ultrastructure of the cells of luminous bacteria and increases luciferase biosynthesis two- to three-fold compared to a control.

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

Доп.точки доступа:
Rodicheva, E.K.; Trubachev, I.N.; Medvedeva, S.E.; Egorova, O.I.; , U - Shitova LYu

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Luminescence of Ca(2+)-activated photoprotein obelin initiated by NaOCl and MnCl2. / E. S. Vysotski [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P301-305 . - ISSN 0884-3996
Кл.слова (ненормированные):
calcium -- chloride -- hypochlorite sodium -- manganese chloride -- manganese derivative -- obelin -- photoprotein -- article -- chemistry -- drug effect -- kinetics -- luminescence -- metabolism -- Calcium -- Chlorides -- Kinetics -- Luminescence -- Luminescent Proteins -- Manganese Compounds -- Sodium Hypochlorite
Аннотация: The luminescence of obelin is initiated by NaOCl in a reaction mixture containing no calcium. The addition of Mn2+ enhances the light emission > 300-fold. Sodium azide and histidine, as singlet oxygen quenchers, inhibit NaOCl-activated obelin luminescence in the presence or absence of Mn2+. This suggests that the addition of NaOCl to the mixture causes singlet oxygen formation (stimulated by Mn2+ ions), and singlet oxygen initiates the light-emitting reaction.

Scopus
Держатели документа:
Laboratory of Photobiology, Russian Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Trofimov, K.P.; Bondar', V.S.; Gitelson, J.I.

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Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemistry. - 1995. - Vol. 34, Is. 10. - P3300-3309 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- recombinant protein -- article -- ligand binding -- nonhuman -- priority journal -- protein isolation -- protein protein interaction -- protein stability -- vibrionaceae -- Bacterial Proteins -- Binding Sites -- Carrier Proteins -- Circular Dichroism -- Flavin Mononucleotide -- Fluorescence Polarization -- Genes, Bacterial -- Kinetics -- Ligands -- Luciferase -- Luminescence -- Molecular Sequence Data -- Photobacterium -- Recombinant Proteins -- Spectrophotometry -- Support, U.S. Gov't, P.H.S. -- Photobacterium leiognathi -- Vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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10.

Interaction of Photobacterium leiognathi and Vibrio fischeri Y1 luciferases with fluorescent (Antenna) proteins: Bioluminescence effects of the aliphatic additive [Text] / V. N. Petushkov [et al.] // Biochemistry. - 1996. - Vol. 35, Is. 37. - P12086-12093, DOI 10.1021/bi9608931. - Cited References: 41 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
BACTERIAL LUCIFERASE
   LUMAZINE PROTEIN
   FLAVIN INTERMEDIATE
   ANGSTROM RESOLUTION
   RIBOFLAVIN PROTEIN
   PURIFICATION
   MECHANISM
   EMISSION
   ALDEHYDE
   INHIBITION
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 call 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, when 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 or the protein-protein interaction in the absence of the aliphatic component.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOL BIOL,ATHENS,GA 30602
RUSSIAN ACAD SCI,INST BIOPHYS,SIBERIAN BRANCH,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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11.

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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12.

Removal of essential ligand in N-terminal calcium binding domain of obelin does not inactivate the photoprotein or reduce its calcium sensitivity, but dramatically alters the kinetics of the luminescent reaction [Text] / V. A. Illarionova [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). - P431-434. - Cited References: 0 . - 4. - ISBN 0-471-97502-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Illarionova, V.A.; Illarionov, B.A.; Bondar, V.S.; Vysotski, E.S.; Blinks, J.R.; Hastings, JW \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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13.

The effect of algal blooms on the disappearance of phenol in a small forest pond / M. I. Gladyshev [et al.] // Water Research. - 1998. - Vol. 32, Is. 9. - P2769-2775, DOI 10.1016/S0043-1354(98)00009-8 . - ISSN 0043-1354
Кл.слова (ненормированные):
Algal blooms -- Phenol -- Seasonal dynamics of biodegradation -- Self-purification -- Algae -- Biodegradation -- Ecosystems -- Phenols -- Purification -- Reaction kinetics -- Reservoirs (water) -- Surface waters -- Experimental microecosystems -- Forest pond waters -- Green algae Volvox aureus -- Inorganic nutrients -- Krasnoyarsk reservoir -- Water pollution -- lake water -- phenol -- article -- ecosystem -- forest -- green alga -- priority journal -- russian federation -- water pollutant -- water temperature
Аннотация: Using experimental microecosystems the kinetics of phenol disappearance in small forest pond waters (Siberia, Russia) in the summer of 1995-96 were investigated. Despite of high variability of components of the ecosystem (plankton biomass and species composition) and two pronounced 'blooms' of green algae Volvox aureus the same kinetics of the disappearance took place over the investigated period. Half-lives of the pollutant depended on water temperature only. A comparison of the self-purification of the pond with that of the Krasnoyarsk reservoir, 'blooming' with blue-greens was carried out. Half-lives in the pond were significantly lower than that in the reservoir. During the periods of 'blooms' of the green algae in the pond the concentrations of inorganic nutrients were comparatively high and the phenol-degrading bacteria likely were not limited by these nutrients, in contrast to the periods of 'bloom' of the blue-green algae in the reservoir.

Scopus
Держатели документа:
Inst. Biophys. Siberian Br. Russ. A., Akademgorodok, 660036, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gladyshev, M.I.; Sushchik, N.N.; Kalachova, G.S.; Shchur, L.A.

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14.

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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15.

DNA synthesis in heterokaryons obtained by fusion of hepatocytes from a regenerating mouse liver and NIH 3T3 fibroblasts / A. V. Eremeev, N. A. Setkov // Doklady Biological Sciences. - 2000. - Vol. 372, Is. 1-6. - P. 329-332 . - ISSN 0012-4966
Кл.слова (ненормированные):
DNA -- thymidine -- animal -- article -- biosynthesis -- cell division -- cell fusion -- cell strain 3T3 -- cytology -- hybrid cell -- kinetics -- liver cell -- liver regeneration -- metabolism -- mouse -- 3T3 Cells -- Animals -- Cell Division -- Cell Fusion -- DNA -- Hepatocytes -- Hybrid Cells -- Kinetics -- Liver Regeneration -- Mice -- Thymidine

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

Доп.точки доступа:
Eremeev, A.V.; Setkov, N.A.

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16.

Kinetic analysis of bacterial water-organic media [Text] / I. E. Sukovataya, N. A. Tyulkova // Luminescence. - 2001. - Vol. 16: 11th International Bioluminescence and Chemiluminescence Symposium (SEP 06-10, 2000, PACIFIC GROVE, CALIFORNIA), Is. 4. - P. 271-273, DOI 10.1002/bio.649.abs. - Cited References: 10 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Кл.слова (ненормированные):
bacterial luciferase -- organic solvents -- Michaelis constant
Аннотация: The interaction of luciferases from two types of luminous bacteria, Photobacterium leiognathi and Vibrio harveyi, with their substrates [the photorecovered. FMNH2 and long-chain aldehydes-decanal (C-10), dodecanal (C-12) and tetradecanal (C-14)] in water-organic media was analysed using kinetic graphical methods. Moderate concentrations of organic solvents have been demonstrated to activate the bioluminescence, while higher concentrations inhibit it. The interactions of these effectors with luciferases show different types of kinetics, which depend on concentrations of solvents, kinds of enzymes and substrates. The apparent value of the Michaelis constant, K-m for C-14 of both luciferases and for C-10 of luciferase V. harveyi is enhanced with increasing concentration of the organic solvent, but K-m for C-12 and C-10 of luciferase P. leiognathi decreases. Obviously, at the specific binding of aldehydes with luciferases in the first case, hydrophobic interactions are realized, but in second, the electrostatic interactions are realized. The series of changes in parameters of bioluminescence reaction catalysed by different luciferases is obviously determined by their structural peculiarities. Copyright (C) 2001 John Wiley & Sons, Ltd.

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

Доп.точки доступа:
Sukovataya, I.E.; Tyulkova, N.A.

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17.

Assessment of 241Am accumulation rate by samples of algobacterial community of the Yenisei River. / A. Y. Bolsunovsky, T. A. Zotina, S. V. Kosinenko // Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections / translated from Russian. - 2002. - Vol. 385. - P374-376 . - ISSN 0012-4966
Кл.слова (ненормированные):
americium -- fresh water -- alga -- animal -- article -- bacterium -- kinetics -- metabolism -- nuclear reactor -- phytoplankton -- Russian Federation -- Algae -- Americium -- Animals -- Bacteria -- Fresh Water -- Kinetics -- Nuclear Reactors -- Phytoplankton -- Russia

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

Доп.точки доступа:
Bolsunovsky, A.Y.; Zotina, T.A.; Kosinenko, S.V.

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18.

Tolerance of LSS plant component to elevated temperatures [Text] / S. A. Ushakova, A. A. Tikhomirov // Acta Astronaut. - 2002. - Vol. 50, Is. 12. - P. 759-764, DOI 10.1016/S0094-5765(02)00010-3. - Cited References: 10 . - ISSN 0094-5765

РУБ Engineering, Aerospace

Аннотация: Stability of LSS based on biological regeneration of water, air and food subject to damaging factors is largely dependent on the behavior of the photosynthesizing component represented, mainly, by higher plants. The purpose of this study is to evaluate the tolerance of uneven-aged wheat and radish cenoses to temperature effects different in time and value. Estimation of thermal tolerance of plants demonstrated that exposure for 20 h to the temperature increasing to 45degreesC brought about irreversible damage both in photosynthetic processes (up to 80% of initial value) and the processes of growth and development. Kinetics of visible photosynthesis during exposure to elevated temperatures can be used to evaluate critical exposure time within the range of which the damage of metabolic processes is reversible. With varying light intensity and air temperature it is possible to find a time period admissible for the plants to stay under adverse conditions without considerable damage of metabolic processes. (C) 2002 Elsevier Science Ltd. All rights reserved.

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

Доп.точки доступа:
Ushakova, S.A.; Tikhomirov, A.A.

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19.

Ca(2+)-activator of the luminescence system of the earthworms Henlea sp., (Annelida: Clitellata: Oligochaeta: Enchytraeidae) / N. S. Rodionova, V. S. Bondar, V. N. Petushkov // Doklady. Biochemistry and biophysics. - 2002. - Vol. 386. - P260-263 . - ISSN 1607-6729
Кл.слова (ненормированные):
calcium -- divalent cation -- edetic acid -- luciferase -- luciferin -- metal -- animal -- annelid worm -- article -- chemistry -- dose response -- enzymology -- genetics -- kinetics -- luminescence -- metabolism -- Animals -- Calcium -- Cations, Divalent -- Dose-Response Relationship, Drug -- Edetic Acid -- Firefly Luciferin -- Kinetics -- Luciferases -- Luminescent Measurements -- Metals -- Oligochaeta

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

Доп.точки доступа:
Rodionova, N.S.; Bondar, V.S.; Petushkov, V.N.

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20.

Obelin from the bioluminescent marine hydroid Obelia geniculata: Cloning, expression, and comparison of some properties with those of other Ca2+-regulated photoproteins [Text] / S. V. Markova [et al.] // Biochemistry. - 2002. - Vol. 41, Is. 7. - P2227-2236, DOI 10.1021/bi0117910. - Cited References: 54 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
AMINO-ACID-SEQUENCE
   CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   CA-2+-ACTIVATED PHOTOPROTEIN
   LUMINESCENT PROTEIN
   BINDING-PROTEIN
   BEROE-OVATA
   AEQUORIN
   CDNA
   PURIFICATION
Аннотация: A cDNA encoding the Ca2+-regulated photoprotein of the bioluminescent marine hydroid Obelia geniculata was cloned and sequenced. The cDNA is a 774 bp fragment containing two overlapping open reading frames, one of which contained 585 bp encoding a 195 amino acid polypeptide which obviously has the primary structure of the apoprotein of a calcium-regulated photoprotein. Many of the residues are identical to those in other Ca2+-regulated photoproteins: 86% compared with that from Obelia longissima, 76% with that from Clytia (Phialidium), 64% with that from Aequorea, and 64% with that from Mitrocoma (Halistaura). The obelin from O. geniculata was overexpressed in Escherichia coli, refolded from inclusion bodies, and purified. The yield of highly purified recombinant protein was 55-80 mg/L of LB medium. O. geniculata obelin has absorption maxima at 280 and 460 nm and a shoulder at approximately 310 nm. The calcium-discharged protein loses visible absorption but exhibits a new absorption maximum at 343 nm. The bioluminescence of the obelin from O. geniculata is blue (lambda(max) = 495 nm). In contrast, the fluorescence of the calcium-discharged protein is yellow-green (lambda(max) = 520 nm; excitation at 340 nm). This is in sharp contrast to aequorin in which the bioluminescence and fluorescence emission spectra of the calcium-discharged protein are almost identical (lambda(max) = 465 nm). The Ca2+ concentration-effect curve for O. geniculata obelin is similar to those of many other photoproteins: at [Ca2+] below approximately 10(-8) M, calcium-independent luminescence is observed, and at [Ca2+] approximately 10(-3) M, the luminescence reaches a maximum. Between these extremes, the curve spans a vertical range of almost 8 log units with a maximum slope on a log-log plot of about 2.5. In the absence of Mg2+ the rate constant for the rise of bioluminescence determined by the stopped-flow technique is about 450 s(-1). The effects of Mg2+ on the kinetics of bioluminescence are complicated, but at all concentrations studied they are relatively small compared to the corresponding effects on aequorin luminescence. At least with respect to speed and sensitivity to Mg2+, the obelins from both O. longissima and O. geniculata would appear to be more suitable than aequorin for use as intracellular Ca2+ indicators.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
Univ Washington, Friday Harbor Labs, Friday Harbor, WA 98250 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Vysotski, E.S.; Blinks, J.R.; Burakova, L.P.; Wang, B.C.; Lee, J...

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