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1.


   
    THE WAY OF SYNTHESIS OF LUCIFERASE ALDEHYDE FACTOR IN PHOTOBACTERIUM MANDAPAMENSIS AND THE INFLUENCE OF ALDEHYDE PRECURSORS ON THE LUMINESCENCE DEVELOPMENT [Текст] / A. N. SHENDEROV, L. Y. POPOVA // Genetika. - 1980. - Vol. 16, Is. 6. - P. 1109-1112. - Cited References: 7 . - ISSN 0016-6758
РУБ Genetics & Heredity


WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
SHENDEROV, A.N.; POPOVA, L.Y.

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2.


   
    Conflict: induction-inhibition of transgene bacteria luminescence in studying expression of lux-genes / D. V. Lesniak, L. I. Popova // Biofizika. - 2002. - Vol. 47, Is. 6. - P. 1059-1063 . - ISSN 0006-3029
Кл.слова (ненормированные):
naphthalene derivative -- salicylic acid derivative -- article -- bacterial gene -- chemistry -- chemoluminescence -- culture medium -- Escherichia coli -- gene expression regulation -- genetics -- metabolism -- Pseudomonas fluorescens -- transgene -- Chemiluminescent Measurements -- Culture Media -- Escherichia coli -- Gene Expression Regulation, Bacterial -- Genes, Bacterial -- Naphthalenes -- Pseudomonas fluorescens -- Salicylates -- Transgenes
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.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Division, Russian Academy of Sciences, Krasnoyarsk-36, Akademgorodok, 660036 Russia. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Lesniak, D.V.; Popova, L.I.

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3.


   
    Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene / A. A. Raibekas // Journal of bioluminescence and chemiluminescence. - 1991. - Vol. 6, Is. 3. - P. 169-176 . - ISSN 0884-3996
Кл.слова (ненормированные):
bacterial protein -- flavoprotein -- amino acid sequence -- article -- bacterial gene -- chemistry -- genetics -- isolation and purification -- luminescence -- molecular genetics -- molecular weight -- Photobacterium -- Amino Acid Sequence -- Bacterial Proteins -- Flavoproteins -- Genes, Bacterial -- Luminescence -- Molecular Sequence Data -- Molecular Weight -- Photobacterium -- Support, U.S. Gov't, P.H.S.
Аннотация: A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.

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

Доп.точки доступа:
Raibekas, A.A.

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4.


   
    NADPH-DEPENDENT AND ATP-DEPENDENT LUMINESCENCE OF EXTRACTS OF LUMINESCENT BACTERIA [Text] / E. S. VYSOTSKII, V. V. ZAVORUEV, V. V. MEZHEVIKIN // Biochem.-Moscow. - 1982. - Vol. 47, Is. 12. - P. 1682-1686. - Cited References: 10 . - ISSN 0006-2979
РУБ Biochemistry & Molecular Biology


WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
VYSOTSKII, E.S.; ZAVORUEV, V.V.; MEZHEVIKIN, V.V.

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5.


   
    THE QUANTUM YIELD OF BACTERIAL LUMINESCENCE [Text] / E. S. VYSOTSKII, E. K. RODICHEVA, G. Y. SHCHERBAKOVA // Microbiology. - 1981. - Vol. 50, Is. 4. - P. 419-422. - Cited References: 15 . - ISSN 0026-2617
РУБ Microbiology


WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
VYSOTSKII, E.S.; RODICHEVA, E.K.; SHCHERBAKOVA, G.Y.

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6.


   
    STUDY OF THE MECHANISM OF THE ACTION OF 2,4-DINITROFLUOROBENZENE ON BACTERIAL LUMINESCENCE INVITRO [Text] / V. A. KRATASYUK, A. M. FISH // Biochem.-Moscow. - 1980. - Vol. 45, Is. 7. - P. 895-900. - Cited References: 13 . - ISSN 0006-2979
РУБ Biochemistry & Molecular Biology


WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
KRATASYUK, V.A.; FISH, A.M.

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7.


   
    Bioluminescence as a tool for study Mechanisms of Radiation Hormesis and Radiation Toxicity [Text] / N. . Kudryasheva [et al.] // Luminescence. - 2014. - Vol. 29. - P26-27. - Cited References: 6 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
SYSTEMS
   AM-241


WOS
Держатели документа:
[Kudryasheva, Nadezhda
Selivanova, Maria] RAS, Inst Biophys Sb, Krasnoyarsk, Russia
[Kudryasheva, Nadezhda
Petrova, Alena
Rozhko, Tatiana] Siberian Fed Univ, Krasnoyarsk, Russia
[Tugarova, Anna
Kamnev, Alexander] RAS, Inst Biochem & Physiol Plants & Microorganisms, Saratov, Russia
[Devyatlovskaya, Anna] State Technol Univ Lb, Lesosibirsk, Krasnoyarsk Reg, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N...; Selivanova, M...; Petrova, A...; Rozhko, T...; Tugarova, A...; Kamnev, A...; Devyatlovskaya, A...

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8.


   
    The production of highly active recombinant 16.5 kDa-isoform of Metridia longa luciferase, the smallest copepod luciferase [Text] / M. . Larionova [et al.] // Luminescence. - 2014. - Vol. 29. - P79-80. - Cited References: 3 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
EXPRESSION

WOS
Держатели документа:
[Larionova, Marina
Markova, Svetlana
Burakova, Ludmila
Vysotski, Eugene] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk, Russia
[Larionova, Marina] Siberian Fed Univ, Inst Fundamental Biol & Biotecnol, Lab Bioluminescence Biotechnol, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Larionova, M...; Markova, S...; Burakova, L...; Vysotski, E...

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9.


   
    A novel ATP-dependent bioluminescent system from the Siberian earthworm Fridericia heliota: structure elucidation of luciferin and its analogs [Text] / V. . Petushkov [et al.] // Luminescence. - 2014. - Vol. 29. - P54-55. - Cited References: 3 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Dubinnyi, Maxim
Tsarkova, Aleksandra
Baranov, Mikhail
Yampolsky, Ilia] Russian Acad Sci, Inst Bioorgan Chem, Moscow, Russia
[Petushkov, Valentin
Rodionova, Natalja
Shimomura, Osamu] Russian Acad Sci, Inst Biophys, Lab Photobiol, Siberian Branch, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V...; Dubinnyi, M...; Tsarkova, A...; Rodionova, N...; Baranov, M...; Shimomura, O...; Yampolsky, I...

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10.


   
    Characterization of hydromedusan Ca2+-regulated photoproteins as a tool for measurement of Ca(2+)concentration [Text] / N. P. Malikova [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5715-5726, DOI 10.1007/s00216-014-7986-2. - Cited References: 67. - This work was supported by RFBR grant 12-04-00131, by the programs of the Government of the Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058) and "Molecular and Cellular Biology" of the Russian Academy of Sciences, and the grant from the President of the Russian Federation "Leading Science School" (3951.2012.4). . - ISSN 1618-2642. - ISSN 1618-2650
РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
LIGHT-SENSITIVE PHOTOPROTEIN
   CTENOPHORE BEROE ABYSSICOLA

   GREEN-FLUORESCENT PROTEIN

   INTRACELLULAR CALCIUM

   SEQUENCE-ANALYSIS

   CA-2+-ACTIVATED PHOTOPROTEIN

   CA2+-BINDING PHOTOPROTEIN

   SEMISYNTHETIC AEQUORINS

   LUMINESCENT PROTEIN

   RECOMBINANT OBELIN

Кл.слова (ненормированные):
Calcium -- Coelenterazine -- Aequorin -- Obelin -- Clytin -- Mitrocomin
Аннотация: Calcium ion is a ubiquitous intracellular messenger, performing this function in many eukaryotic cells. To understand calcium regulation mechanisms and how disturbances of these mechanisms are associated with disease states, it is necessary to measure calcium inside cells. Ca2+-regulated photoproteins have been successfully used for this purpose for many years. Here we report the results of comparative studies on the properties of recombinant aequorin from Aequorea victoria, recombinant obelins from Obelia geniculata and Obelia longissima, recombinant mitrocomin from Mitrocoma cellularia, and recombinant clytin from Clytia gregaria as intracellular calcium indicators in a set of identical in vitro and in vivo experiments. Although photoproteins reveal a high degree of identity of amino acid sequences and spatial structures, and, apparently, have a common mechanism for the bioluminescence reaction, they were found to differ in the Ca2+ concentration detection limit, the sensitivity of bioluminescence to Mg2+, and the rates of the rise of the luminescence signal with a sudden change of Ca2+ concentration. In addition, the bioluminescence activities of Chinese hamster ovary cells expressing wild-type photoproteins also differed. The light signals of cells expressing mitrocomin, for example, slightly exceeded the background, suggesting that mitrocomin may be hardly used to detect intracellular Ca2+ without modifications improving its properties. On the basis of experiments on the activation of endogenous P2Y(2) receptor in Chinese hamster ovary cells by ATP, we suggest that wild-type aequorin and obelin from O. longissima are more suitable for calcium detection in cytoplasm, whereas clytin and obelin from O. geniculata can be used for calcium measurement in cell compartments with high Ca2+ concentration.

WOS
Держатели документа:
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Malikova, Natalia P.
Burakova, Ludmila P.
Markova, Svetlana V.
Vysotski, Eugene S.] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Malikova, N.P.; Burakova, L.P.; Markova, S.V.; Vysotski, E.S.; RFBR [12-04-00131]; Government of the Russian Federation [11.G34.31.0058]; Russian Academy of Sciences; Russian Federation "Leading Science School" [3951.2012.4]

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11.


   
    Isolation of luminescence system from the luminescent fungus Neonothopanus nambi [Text] / V. S. Bondar [et al.] // Dokl. Biochem. Biophys. - 2014. - Vol. 455, Is. 1. - P56-58, DOI 10.1134/S1607672914020045. - Cited References: 10. - This study was supported by the Program of the Government of the Russian Federation "On Measures to Attract the Leading Scientists to the Educational Institutions of Russia" (project no. 11, G34.31.0058) and the Siberian Branch of the Russian Academy of Sciences (project no. 71). . - ISSN 1607-6729. - ISSN 1608-3091
РУБ Biochemistry & Molecular Biology + Biophysics


WOS
Держатели документа:
[Bondar, V. S.
Puzyr', A. P.
Purtov, K. V.
Petunin, A. I.
Rodicheva, E. K.
Medvedeva, S. E.
Gitel'zon, I. I.] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Bondar, V. S.
Puzyr', A. P.
Purtov, K. V.
Burov, A. E.
Rodicheva, E. K.
Medvedeva, S. E.
Shpak, B. A.
Tyaglik, A. B.
Shimomura, O.
Gitel'zon, I. I.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Burov, A. E.] Russian Acad Sci, Nauka Special Design & Technol Bur, Krasnoyarsk Sci Ctr, Siberian Branch, Krasnoyarsk, Russia
[Shimomura, O.] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН
СКТБ Наука : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Bondar, V.S.; Puzyr', A.P.; Purtov, K.V.; Petunin, A.I.; Burov, A.E.; Rodicheva, E.K.; Medvedeva, S.E.; Shpak, B.A.; Tyaglik, A.B.; Shimomura, O...; Gitel'zon, I.I.; Program of the Government of the Russian Federation "On Measures to Attract the Leading Scientists to the Educational Institutions of Russia" [11, G34.31.0058]; Siberian Branch of the Russian Academy of Sciences [71]

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12.


   
    Application of enzyme bioluminescence in ecology [Text] / V. . Kratasyuk, E. . Esimbekova // Luminescence. - 2014. - Vol. 29. - P25-25. - Cited References: 6 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
SYSTEM
   WATER

   ASSAY


WOS
Держатели документа:
[Kratasyuk, Valentina
Esimbekova, Elena] Siberian Fed Univ, Krasnoyarsk, Russia
[Kratasyuk, Valentina
Esimbekova, Elena] RAS, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kratasyuk, V...; Esimbekova, E...

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13.


   
    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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14.


   
    THE LOCALIZATION OF LUMINESCENT SYSTEM OF LUMINOUS BACTERIA [Текст] / O. A. KUDRYAVTSEVA [и др.] // Biofizika. - 1993. - Vol. 38, Is. 3. - P. 435-439. - Cited References: 10 . - ISSN 0006-3029
РУБ Biophysics

Аннотация: A method for localization of a light source near the interface of two media is described. The method is based on an optical analog of tunnel effect when the radiation source is at the distance smaller than the wavelength from the interface. Application of the tunnel effect permits to obtain high resolution. The developed method was used to determine the localization of a bacterial luminescent system. It has been found that the sources of bioluminescence are located at thin subsurfase lager with width about 70 nm. This result is in favour of the peripheral (periplasmatic or membrane) localization of the bacterial luminescent system. This method makes it possible to investigate processes pelated to light radiation (luminescence, fluorescence and other optical processes) in a thin surface layer of various biological and physical objects.

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

Доп.точки доступа:
KUDRYAVTSEVA, O.A.; BARTSEV, S.I.; OKHONIN, V.A.; MEZHEVIKIN, V.V.

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15.


   
    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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16.


   
    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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17.


   
    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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18.


   
    Controlled expression of bacterial luminescence genes cloned in a multicopy recombinant plasmid [Text] / E. E. Maksimova [et al.] // Microbiology. - 1997. - Vol. 66, Is. 2. - P. 184-187. - Cited References: 17 . - ISSN 0026-2617
РУБ Microbiology
Рубрики:
GENETICALLY-MODIFIED MICROORGANISMS
   BIOLUMINESCENCE

   ENVIRONMENT

Кл.слова (ненормированные):
recombinant plasmid -- Escherichia coli -- luminescence -- catabolite repression
Аннотация: Luminescence and growth responses of the recombinant strain Escherichia coil Z905 (Ap(r)Lux(+)) to different concentrations of ampicillin depended on the source of carbon and energy. When glycerol was used as the substrate, the intensity of luminescence rose with the ampicillin concentration in the medium. Glucose caused catabolite repression of cell luminescence up to the late stationary phase, and ampicillin enhanced this effect. The feasibility of controlling the expression of cloned lux genes was shown.

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

Доп.точки доступа:
Maksimova, E.E.; Popova, L.Y.; Kargatova, T.V.; Shpagina, V.V.

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19.


   
    THE ABSENCE OF MAGNETIC-FIELD INFLUENCE ON BACTERIAL LUMINESCENCE INTENSITY [Текст] / V. N. PETUSHKOV // Biofizika. - 1985. - Vol. 30, Is. 2. - P. 349-351. - Cited References: 10 . - ISSN 0006-3029
РУБ Biophysics


WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
PETUSHKOV, V.N.

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20.


   
    CHANGES IN PERIPLASMIC SPACE OF LUMINESCENT BACTERIA AS A FUNCTION OF LUMINESCENCE INTENSITY [Text] / M. V. SALNIKOV [et al.] // Microbiology. - 1984. - Vol. 53, Is. 5. - P. 606-609. - Cited References: 8 . - ISSN 0026-2617
РУБ Microbiology


WOS : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
SALNIKOV, M.V.; VYSOTSKII, E.S.; ZAVORUEV, V.V.; MEZHEVIKIN, V.V.

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