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Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (6)

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A new enzymatic technique to estimate the efficiency of microbial degradation of pollutants / A. B. Sarangova, L. A. Somova // Advances in Space Research. - 1997. - Vol. 20, Is. 10. - P2049-2052 . - ISSN 0273-1177
Кл.слова (ненормированные):
catalase -- hydrogen peroxide -- aerobic metabolism -- article -- bacterium -- biomass -- bioremediation -- enzymology -- metabolism -- methodology -- microbiology -- sewage -- waste management -- water management -- Aerobiosis -- Bacteria -- Biodegradation, Environmental -- Biomass -- Catalase -- Hydrogen Peroxide -- Sewage -- Waste Management -- Water Microbiology -- Water Purification
Аннотация: Dynamics of active sludge microorganism activity in aerotanks under chemostat conditions has been studied. Dependence of microorganism catalase activity has been found to depend on residual substrate concentration in proportion to the biomass of microorganisms. Experimental data and field observations has formed the basis to develop a technique to evaluate in relative units the amount of the substrate consumed by biocenosis of the active sludge in the air tanks of purification facilities. В© 1997 COSPAR. Published by Elsevier Science Ltd.

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

Доп.точки доступа:
Sarangova, A.B.; Somova, L.A.

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Catalase activity as a potential indicator of the reducer component of small closed ecosystems / A. B. Sarangova, L. A. Somova, T. I. Pisman // Advances in Space Research. - 1997. - Vol. 20, Is. 10. - P1945-1948 . - ISSN 0273-1177
Кл.слова (ненормированные):
carboxymethylcellulose -- catalase -- animal -- article -- Bacillus -- bacterial count -- Chlorella -- culture medium -- enzymology -- growth, development and aging -- metabolism -- microclimate -- Paramecium -- Animals -- Bacillus -- Carboxymethylcellulose -- Catalase -- Chlorella -- Colony Count, Microbial -- Culture Media -- Ecological Systems, Closed -- Paramecium
Аннотация: Dynamics of catalase activity has been shown to reflect the growth curve of microorganisms in batch cultivation (celluloselythic bacteria Bacillus acidocaldarius and bacteria of the associated microflora Chlorella vulgaris). Gas and substrate closure of the three component ecosystems with spatially separated components "producer-consumer-reducer" (Chl. vulgaris-Paramecium caudatum-B. acidocaldarius, two bacterial strains isolated from the associated microflora Chl. vulgaris) demonstrated that the functioning of the reducer component can be estimated by the catalase activity of microorganisms of this component. В© 1997 COSPAR. Published by Elsevier Science Ltd.

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

Доп.точки доступа:
Sarangova, A.B.; Somova, L.A.; Pisman, T.I.

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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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Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator [Text] / B. A. Illarionov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P223-249. - Cited References: 58 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
PHOTOPROTEIN OBELIN
   MESSENGER-RNA
   CA-2+-ACTIVATED PHOTOPROTEIN
   DIRECTED MUTAGENESIS
   SEQUENCE-ANALYSIS
   HYDROID OBELIA
   AEQUORIN
   PROTEIN
   BIOLUMINESCENCE
   LUMINESCENCE

Держатели документа:
Russian Acad Sci, Inst Biophys, Photobiol Lab, 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:
Illarionov, B.A.; Frank, L.A.; Illarionova, V.A.; Bondar, V.S.; Vysotski, E.S.; Blinks, J.R.

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Purification and ligand exchange protocols for antenna proteins from bioluminescent bacteria [Text] / V. N. Petrushkov [et al.] // Methods Enzymol. - 2000. - Vol. 305. - P. 164-180. - Cited References: 18 . - ISSN 0076-6879

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology
Рубрики:
YELLOW FLUORESCENT PROTEIN
   FISCHERI STRAIN Y-1
   AMINO-ACID-SEQUENCE
   VIBRIO-FISCHERI
   PHOTOBACTERIUM-LEIOGNATHI
   RIBOFLAVIN PROTEIN
   LUMINOUS BACTERIUM
   LUMAZINE PROTEIN
   FMN
   Y1

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Agr Univ Wageningen, Dept Biochem, NL-6703 HA Wageningen, Netherlands
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petrushkov, V.N.; Gibson, B.G.; Visser, AJWG; Lee, J...

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On monitoring the bacterial component as an indicator of the state of small man-made ecosystems / A. B. Sarangova, L. A. Somova, N. S. Pechurkin // Advances in Space Research. - 2001. - Vol. 27, Is. 9. - P1605-1609, DOI 10.1016/S0273-1177(01)00256-3 . - ISSN 0273-1177
Кл.слова (ненормированные):
Bacteria -- Ecosystems -- Substrates -- Intracellular substrate concentration -- Space research -- catalase -- oxidoreductase -- artificial ecosystem -- article -- bacterial phenomena and functions -- biomass -- culture medium -- ecosystem -- enzymology -- growth, development and aging -- metabolism -- microbiology -- oxygen consumption -- Pseudomonas -- Bacterial Physiology -- Biomass -- Catalase -- Culture Media -- Ecosystem -- Oxidoreductases -- Oxygen Consumption -- Pseudomonas -- Water Microbiology
Аннотация: High reproduction rates make the bacterial component of ecosystems a good indicator of the state of the system on the whole. This determines the necessity to develop rapid monitoring of the functional state of the bacterial component of small ecosystems. Information about substrate concentration in the population is indicative of the state of the bacterial culture. Conventional methods of monitoring the concentration of integral substrate in the system take time much longer than the changes in the ecosystem. The paper presents theoretical foundations for the logical sequence "catalase activity - intracellular substrate concentration - estimate of substrate consumed by bacteria" for experimental verification and as a consequence of development of the integral method of monitoring the bacterial population on the basis of determining bacterial catalase activity. В© 2001 COSPAR. Published by Elsevier Science Ltd. All rights reserved.

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

Доп.точки доступа:
Sarangova, A.B.; Somova, L.A.; Pechurkin, N.S.

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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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Dynamics of activity of the key enzymes of polyhydroxyalkanoate metabolism in Ralstonia eutropha / T. G. Volova [и др.] // Prikladnaia biokhimiia i mikrobiologiia. - 2004. - Vol. 40, Is. 2. - С. 201-209 . - ISSN 0555-1099
Кл.слова (ненормированные):
acetoacetyl coenzyme a reductase -- acetoacetyl-CoA reductase -- acetyl coenzyme A acyltransferase -- acyltransferase -- alcohol dehydrogenase -- carboxylesterase -- hydroxybutyrate dehydrogenase -- hydroxybutyric acid -- poly(3 hydroxyalkanoic acid) depolymerase -- poly(3-hydroxyalkanoic acid) depolymerase -- poly(3-hydroxyalkanoic acid) synthase -- polyhydroxyalkanoate synthase -- polymer -- article -- chemistry -- comparative study -- culture medium -- enzymology -- growth, development and aging -- metabolism -- Wautersia eutropha -- Acetyl-CoA C-Acyltransferase -- Acyltransferases -- Alcohol Oxidoreductases -- Carboxylic Ester Hydrolases -- Culture Media -- Cupriavidus necator -- Hydroxybutyrate Dehydrogenase -- Hydroxybutyrates -- Polymers
Аннотация: The dynamics of accumulation of polyhydroxybutyrate (PHB) and the activities of the key enzymes of PHB metabolism (beta-ketothiolase, acetoacetyl-CoA reductase, PHA synthase, D-hydroxybutyrate dehydrogenase, and PHA depolymerase) in the hydrogen bacterium Ralstonia eutropha B5786 were studied under various conditions of carbon nutrition and substrate availability. The highest activities of beta-ketothiolase, acetoacetyl-CoA reductase, and PHA synthase were recorded at the stage of acceleration of PHB synthesis. The activities of enzymes catalyzing PHB depolymerization (PHB depolymerase and D-hydroxybutyrate dehydrogenase) were low, being expressed only at stimulated endogenous PHB degradation. The change of carbon source (CO2 or fructose) did not cause any marked changes in the time course of enzyme activity.

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:
Volova, T.G.; Kalacheva, G.S.; Gorbunova, O.V.; Zhila, N.O.

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Untangling metabolic and spatial interactions of stress tolerance in plants. 1. Patterns of carbon metabolism within leaves / K. Y. Biel [et al.] // Protoplasma. - 2010. - Vol. 245, Is. 1. - P49-73, DOI 10.1007/s00709-010-0135-7 . - ISSN 0033-183X
Кл.слова (ненормированные):
Carbon metabolism -- Leaf anatomy -- Leaf form and function -- Maximal ecological utility -- Photosynthesis -- Stress tolerance Spinacia oleracea -- aspartate aminotransferase isoenzyme 1 -- bicarbonate -- carbon -- carbon dioxide -- catalase -- chlorophyll -- malate dehydrogenase -- oxygen -- ribulosebisphosphate carboxylase -- vegetable protein -- article -- enzymology -- histology -- light -- metabolism -- oxidation reduction reaction -- photosynthesis -- physiological stress -- physiology -- plant leaf -- spinach -- theoretical model -- Aspartate Aminotransferase, Cytoplasmic -- Bicarbonates -- Carbon -- Carbon Dioxide -- Catalase -- Chlorophyll -- Light -- Malate Dehydrogenase -- Models, Theoretical -- Oxidation-Reduction -- Oxygen -- Photosynthesis -- Plant Leaves -- Plant Proteins -- Ribulose-Bisphosphate Carboxylase -- Spinacia oleracea -- Stress, Physiological -- Spinacia oleracea
Аннотация: The localization of the key photoreductive and oxidative processes and some stress-protective reactions within leaves of mesophytic C3 plants were investigated. The role of light in determining the profile of Rubisco, glutamate oxaloacetate transaminase, catalase, fumarase, and cytochrome-c-oxidase across spinach leaves was examined by exposing leaves to illumination on either the adaxial or abaxial leaf surfaces. Oxygen evolution in fresh paradermal leaf sections and CO2 gas exchange in whole leaves under adaxial or abaxial illumination was also examined. The results showed that the palisade mesophyll is responsible for the midday depression of photosynthesis in spinach leaves. The photosynthetic apparatus was more sensitive to the light environment than the respiratory apparatus. Additionally, examination of the paradermal leaf sections by optical microscopy allowed us to describe two new types of parenchyma in spinach-pirum mesophyll and pillow spongy mesophyll. A hypothesis that oxaloacetate may protect the upper leaf tissue from the destructive influence of active oxygen is presented. The application of mathematical modeling shows that the pattern of enzymatic distribution across leaves abides by the principle of maximal ecological utility. Light regulation of carbon metabolism across leaves is discussed. В© 2010 Springer-Verlag.

Scopus
Держатели документа:
Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russian Federation
Biosphere Systems International Foundation, Oro Valley, AZ 85755, United States
International Scientific Centre for Organism Extreme States Research, Krasnoyarsk Scientific Centre, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Forest, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Biocompatible Plant Research Institute, College of Natural Sciences, California State University, Chico, CA 95929-0555, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Biel, K.Y.; Fomina, I.R.; Nazarova, G.N.; Soukhovolsky, V.G.; Khlebopros, R.G.; Nishio, J.N.

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