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Dynamic model of the haeme-haeme interaction / I. I. Gitel'zon, T. P. Sandalova, Yu. A. Kudenko // Biophysics. - 1973. - Vol. 18, Is. 4. - P804-807 . - ISSN 0006-3509
Аннотация: The possibility of explaining the acceleration of the reaction of oxygenation of haemoglobin from studying the thermodynamic properties of the molecular chains of haemoglobin present in contact with each other is considered. В© 1974.

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

Доп.точки доступа:
Gitel'zon, I.I.; Sandalova, T.P.; Kudenko, Yu.A.

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Kinetic features of switching of bacterial luciferase from one aldehyde substrate to another / N. S. Rodionova, V. N. Petushkov, P. I. Belobrov // Biophysics. - 1988. - Vol. 33, Is. 3. - P424-430 . - ISSN 0006-3509
Аннотация: In luciferase isolated from luminescing bacteria Vibrio harveyi the authors have studied the dynamics of the luminescence with aliphatic aldehydes C10, C12 and C14 taken in pairs in the reaction with photoreduced flavin mononucleotide (FMN) and in the conjugated system NAD В· H: :FMN-oxidoreductase-luciferase. The kinetic characteristics of endogenous aldehyde have been determined. It is shown that the process of switching of luciferase from one aldehyde substrate to another is dependent on chain length and the order of introducing the aldehydes into the reaction mixture. Analysis of the "matrix of successive perturbations" gave a numerical matrix of the probabilities of oxidation of the aldehydes in the luminescent reaction. An order of preference of the aldehydes on their binding to luciferase is constructed. В© 1989.

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:
Rodionova, N.S.; Petushkov, V.N.; Belobrov, P.I.

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Bioluminescence in oceanology. / I. I. Gitelson, L. A. Levin // Journal of bioluminescence and chemiluminescence. - 1989. - Vol. 4, Is. 1. - P555-562 . - ISSN 0884-3996
Кл.слова (ненормированные):
article -- biology -- circadian rhythm -- ecology -- gas -- instrumentation -- luminescence -- oceanography -- Circadian Rhythm -- Ecology -- Gases -- Luminescence -- Marine Biology -- Oceanography
Аннотация: For analytical purposes bioluminescence can be used in three main ways: 1. luminescence measurement of bioluminescent system components isolated in vitro; 2. determination of luminous organisms' reaction to the in vivo test-action; 3. measurement of bioluminescence in marine ecological systems. The majority of the reports of this Symposium are dealing with the first two topics. The aim of our presentation is to draw attention to the third one. The possibilities of bioluminescent analysis are wider than its traditional scheme of applications in the laboratory, when the emitting system is withdrawn from a native source and is placed in a cuvette of the light measuring device. The reverse scheme is also possible, i.e. the device can be introduced into light emitting system such as a marine biocenosis--the community of the sea inhabitants--where we obtain a highly sensitive and rapid means of gaining the information on the vital activity of marine ecosystems, i.e. their spatial structure, rhythms, man's influence upon them, etc. The present communication will consider the possibilities of this form of bioluminescent analysis.

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

Доп.точки доступа:
Gitelson, I.I.; Levin, L.A.

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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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CADMIUM-INDUCED LUMINESCENCE OF RECOMBINANT PHOTOPROTEIN OBELIN [Text] / V. S. BONDAR [et al.] // Biochim. Biophys. Acta-Bioenerg. - 1995. - Vol. 1231, Is. 1. - P29-32, DOI 10.1016/0005-2728(95)00059-R. - Cited References: 21 . - ISSN 0005-2728

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
AEQUORIN
Кл.слова (ненормированные):
PHOTOPROTEIN -- OBELIN -- CADMIUM -- BIOLUMINESCENCE
Аннотация: It has been shown for the first time that Cd2+ ions induce substantial bioluminescence of a Ca2+-binding photoprotein: recombinant obelin. The optimum pH for the bioluminescent rr:action in the presence of Cd2+ ions is pH 6. The intensity, L, of the light emission for the Cd2+ ions is 75% of the intensity of the signal in the presence of Ca2+. The quantum yields of the reactions in the presence of Cd2+ and Ca2+ are 0.18 and 0.24 respectively. The slope of the straight line (between 5 and 90% of L,,) in the coordinates of log(L/(L(max) - L)) vs. log([Cd2+]) is 1.75 +/- 0.06, which indicates positive cooperative character of this reaction. At a concentration exceeding 1 . 10(-3) M, Cd2+ inhibits the bioluminescent reaction.

Держатели документа:
AGR UNIV WAGENINGEN,DEPT BIOCHEM,6703 HA WAGENINGEN,NETHERLANDS
RUSSIAN ACAD SCI,INST BIOPHYS,KRASNOYARSK 660036,RUSSIA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; SERGEEV, A.G.; ILLARIONOV, B.A.; VERVOORT, J...; HAGEN, W.R.

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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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Direct measurement of excitation transfer in the protein complex of bacterial luciferase hydroxyflavin and the associated yellow fluorescence proteins from Vibrio fischeri Y1 [Text] / V. N. Petushkov, B. G. Gibson, J. . Lee // Biochemistry. - 1996. - Vol. 35, Is. 25. - P8413-8418, DOI 10.1021/bi952691v. - Cited References: 24 . - ISSN 0006-2960

РУБ Biochemistry & Molecular Biology
Рубрики:
LUMAZINE PROTEIN
   LUMINOUS BACTERIUM
   STRAIN Y-1
   BIOLUMINESCENCE
   EMISSION
   PURIFICATION
   TRANSIENT
   LIGHT
Аннотация: Time-resolved fluorescence was used to directly measure the energy transfer rate constant in the protein-protein complex involved in the yellow bioluminescence of Vibrio fischeri, strain Y1. In this reaction the putative donor is the fluorescent transient intermediate, luciferase hydroxyflavin, which exhibits a major fluorescence lifetime of the bound flavin of 10 ns. On addition of the acceptor, the V. fischeri yellow fluorescence protein containing either FMN or riboflavin as ligand, a rapid decay time, 0.25 ns, becomes predominant. The same results are observed using rec-luciferase from Photobacterium leiognathi to produce the donor. Because of favorable spectral separation in this system, this rapid decay rate of 4 ns(-1), can be directly equated to the energy transfer rate. This rate is ten times higher than the rate previously observed in the Photobacterium luciferase hydroxyflavin-lumazine protein, donor-acceptor system, derived from emission anisotropy measurements. This ten-times ratio is close to the ratio of spectral overlaps of the donor fluorescence with the acceptor absorption, between these two systems, so it is concluded that the topology of the protein complexes in both cases, must be very similar. Energy transfer is also monitored by the loss of steady-state fluorescence intensity at 460 nm of the donor, on addition of the acceptor protein. A fluorescence titration indicates that luciferase hydroxyflavin and the yellow protein complex with a 1:1 stoichiometry with a K-d of 0.7 mu M (0 degrees C). These parameters account for the bioluminescence spectral shifting effects observed in these reactions.

Держатели документа:
UNIV GEORGIA,DEPT BIOCHEM & MOLEC 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.; Gibson, B.G.; Lee, J...

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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.

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.

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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12.

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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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.

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.

WOS
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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15.

On the quenching of bacterial luminescence by dyes [Текст] / Y. P. Meshalkin [и др.] // Biofizika. - 1999. - Vol. 44, Is. 6. - P. 1083-1087. - Cited References: 5 . - ISSN 0006-3029

РУБ Biophysics

Кл.слова (ненормированные):
bacterial luminescence -- dyes -- quenching
Аннотация: It was shown that the addition of dyes (sodium fluorescein, rhodamine 6G, unsubstituted rhodamine) to a bienzymic reaction mixture. (luciferin-luciferase. complex): leads to a decrease: in fluorescence intensity and the appearance of the dye fluorescence band. A similar effect was observed when the luciferin-luciferase complex and dye molecules were separated by distances considerably. exceeding the Forster radius of transfer. It is assumed that the mechanism of dye. fluorescence is not related to the excitation energy resonance transfer but is based on the excitation of dye molecules due to direct absorption of quanta of bacterial bioluminescence.

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

Доп.точки доступа:
Meshalkin, Y.P.; Nemtseva, E.V.; Alfimov, E.E.; Kudryasheva, N.S.

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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.

On the involvement of macrophages and phosphomonoesterases in the tissue response to implantation of polyhydroxyalkanoates. / E. I. Shishatskaya, T. G. Volova, I. I. Gitelson // Doklady Biological Sciences. - 2002. - Vol. 383, Is. 1-6. - P116-119 . - ISSN 0012-4966
Кл.слова (ненормированные):
alkane -- phosphatase -- animal -- article -- comparative study -- foreign body reaction -- macrophage -- metabolism -- physiology -- rat -- Wistar rat -- Alkanes -- Animals -- Foreign-Body Reaction -- Macrophages -- Phosphoric Monoester Hydrolases -- Rats -- Rats, Wistar

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:
Shishatskaya, E.I.; Volova, T.G.; Gitelson, I.I.

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18.

A new scheme of lignin biosynthesis and the mechanism of its regulation of functional properties. / D. A. Semenov, N. E. Sudachkova, R. G. Khlebopros // Doklady. Biochemistry and biophysics. - 2002. - Vol. 382. - P50-52 . - ISSN 1607-6729
Кл.слова (ненормированные):
lignin -- peroxidase -- phenol derivative -- polymer -- article -- biosynthesis -- cell wall -- chemistry -- metabolism -- oxidation reduction reaction -- physiology -- plant -- Cell Wall -- Lignin -- Oxidation-Reduction -- Peroxidase -- Phenols -- Plants -- Polymers

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:
Semenov, D.A.; Sudachkova, N.E.; Khlebopros, R.G.

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19.

A conflict: Induction-inhibition of luminescence in the expression of lux-genes in transgenic bacteria [Текст] / D. V. Lesnyak, L. Y. Popova // Biofizika. - 2002. - Vol. 47, Is. 6. - P. 1059-1063. - Cited References: 12 . - ISSN 0006-3029

РУБ Biophysics

Кл.слова (ненормированные):
salicylate, naphtalene concentration -- bacterial bioluminescence, biodegradation
Аннотация: The relationship between the induction of the luminescent operon of lux-genes fused with the naphthalene and salicylate degradation genes and the inhibition of light emission caused by these compounds was studied. The quantitative correlations between these processes manifest themselves in the fact that light intensity linearly increased in a narrow concentration range of the inductor and then decreased due to the inhibition of the luminescence reaction itself, which is not related to the regulation of expression of lux-genes.

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:
Lesnyak, D.V.; Popova, L.Y.

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20.

Tissue response to biodegradable suture threads made of polyhydroxyalkanoates / E. I. Shishatskaya [et al.] // Biomedical Engineering. - 2002. - Vol. 36, Is. 4. - P210-217, DOI 10.1023/A:1021184119268 . - ISSN 0006-3398
Кл.слова (ненормированные):
acid phosphatase -- alkaline phosphatase -- polyhydroxyalkanoic acid -- animal experiment -- animal tissue -- article -- biocompatibility -- biodegradability -- controlled study -- elasticity -- enzyme activity -- enzyme mechanism -- female -- histochemistry -- incision -- nonhuman -- physical chemistry -- postoperative period -- rat -- rigidity -- suture -- thickness -- tissue reaction -- wound healing -- Animalia

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk Terr. Bur. Pathol. Anat., Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Shishatskaya, E.I.; Volova, T.G.; Efremov, S.N.; Puzyr', A.P.; Mogil'Naya, O.A.

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