Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

в найденном

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=enzymatic<.>)

Общее количество найденных документов : 47
Показаны документы с 1 по 20

1-20 21-40 41-47

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.

Найти похожие

A new enzymatic technique to estimate the efficiency of microbial degradation of pollutants [Text] / A. B. Sarangova, L. A. Somova ; ed. RM Wheeler [et al.] // LIFE SCIENCES: LIFE SUPPORT SYSTEMS STUDIES-I. Ser. ADVANCES IN SPACE RESEARCH : PERGAMON PRESS LTD, 1997. - Vol. 20: F4.6, F4.8, F4.2 and F4.9 Symposia of COSPAR Scientific Commission F on Life Sciences - Life Support System Studies-I, at the 31st COSPAR Scientific Assembly (JUL 14-SEP 21, 1996, BIRMINGHAM, ENGLAND), Is. 10. - P. 2049-2052, DOI 10.1016/S0273-1177(97)00940-X. - Cited References: 4 . - ISBN 0273-1177. - ISBN 0-08-043307-3

РУБ Engineering, Aerospace + Astronomy & Astrophysics + Geosciences, Multidisciplinary + Meteorology & Atmospheric Sciences

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. (C) 1997 COSPAR. Published by Elsevier Science 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:
Sarangova, A.B.; Somova, L.A.; Wheeler, RM \ed.\; Garland, JL \ed.\; Tibbitts, TW \ed.\; Nielsen, SS \ed.\

Найти похожие

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.

Найти похожие

Effects of quinones on NADH-dependent enzymatic bioluminescent systems [Text] / N. S. Kudryasheva [et al.] // Appl. Biochem. Microbiol. - 2000. - Vol. 36, Is. 4. - P. 409-413, DOI 10.1007/BF02738052. - Cited References: 13 . - ISSN 0003-6838

РУБ Biotechnology & Applied Microbiology + Microbiology

Аннотация: The effects of a number of quinones on the bioluminescence characteristics of a three-component enzymatic system containing alcohol dehydrogenase, bacterial luciferase, and NADH-FMN oxidoreductase were studied to find the most sensitive kinetic parameters of the system intended to be used in biological testing. Both direct and back reactions catalyzed by alcohol dehydrogenase were studied in the presence and in the absence of quinones. The kinetic parameters of the bioluminescent system were found to depend on the redox potentials and concentrations of quinones. The quinone-induced effects were shown to be associated with changes in the NAD(+)/NADH ratio in the chain of NADH-dependent enzymes, The three-enzyme system based on alcohol dehydrogenase is suggested as a bioluminescence test for ecological monitoring of waste water.

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk 660036, Russia
Irkutsk State Univ, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kudryasheva, N.S.; Esimbekova, E.N.; Kudinova, I.Y.; Kratasyuk, V.A.; Stom, D.I.

Найти похожие

Role of conservative residue Cys158 in the formation of an active photoprotein complex of obelin [Text] / V. S. Bondar [et al.] // Biochem.-Moscow. - 2001. - Vol. 66, Is. 9. - P1014-1018, DOI 10.1023/A:1012377827626. - Cited References: 21 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CDNA
   EXPRESSION
   AEQUORIN
   SEQUENCE
   CLONING
Кл.слова (ненормированные):
photoproteins -- obelin -- apoobelin mutants -- bioluminescence
Аннотация: Using site directed mutagenesis, the conservative residue Cys158 of recombinant apoobelin was substituted for sera ine (C158S, S-mutant) or alanine (C158A, A-mutant). These point mutations resulted in significant changes in the apoobelin structure accompanied by slowing of photoprotein complex formation, decrease of its stability, and changing of its bioluminescence characteristics. The enzymatic properties of the photoprotein decreased in the series: wild-type protein > S-mutant > A-mutant. This is consistent with rank of nucleophilicity SH > OH > CH3 of cysteine, serine, and alanine side chain functional groups, respectively. Possible mechanisms of the involvement of the apoobelin Cys158 SH-group in the formation of the enzyme-substrate complex are considered.

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

Доп.точки доступа:
Bondar, V.S.; Purtov, K.V.; Malikova, N.P.; Frank, L.A.; Illarionov, B.A.

Найти похожие

Biosynthesis of tetrahydrofolate in plants: Crystal structure of 7,8-dihydroneopterin aldolase from Arabidopsis thaliana reveals a novel adolase class [Text] / S. . Bauer [et al.] // J. Mol. Biol. - 2004. - Vol. 339, Is. 4. - P. 967-979, DOI 10.1016/j.jmb.2004.04.034. - Cited References: 66 . - ISSN 0022-2836

РУБ Biochemistry & Molecular Biology
Рубрики:
GTP CYCLOHYDROLASE-I
   GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE
   6-PYRUVOYL TETRAHYDROPTERIN SYNTHASE
   ESCHERICHIA-COLI
   DIHYDRONEOPTERIN ALDOLASE
   FOLIC-ACID
   ENZYMATIC SYNTHESIS
   DIHYDROPTEROATE SYNTHASE
   REACTION-MECHANISM
   3-DIMENSIONAL STRUCTURE
Кл.слова (ненормированные):
tetrahydrofolate biosynthesis -- aldolase classes -- retroaldol reaction -- purin binding -- Schiff base
Аннотация: Dihydroneopterin aldolase (DHNA) catalyses a retroaldol reaction yielding 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin, tetrahydrofolate. The enzyme is a potential target for antimicrobial and anti-parasite chemotherapy. A gene specifying a dihydroneopterin aldolase from Arabidopsis thaliana was expressed in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity and crystallised using polyethylenglycol as the precipitating agent. The crystal structure was solved by X-ray diffraction analysis at 2.2 Angstrom resolution. The enzyme forms a D-4-symmetric homo-octamer. Each polypeptide chain is folded into a single domain comprising an antiparallel four-stranded beta-sheet and two long alpha-helices. Four monomers are arranged in a tetrameric ring, and two of these rings form a hollow cylinder. Well defined purine derivatives are found at all eight topologically equivalent active sites. The subunit fold of the enzyme is related to substructures of dihydroneopterin triphosphate epimerase, GTP cyclohydrolase I, and pyruvoyltetrahydropterin synthase, which are all involved in the biosynthesis of pteridine type cofactors, and to urate oxidase, although some members of that superfamily have no detectable sequence similarity Due to structural and mechanistical differences of DHNA in comparison with class I and class II aldolases, a new aldolase class is proposed. (C) 2004 Elsevier Ltd. All rights reserved.

WOS
Держатели документа:
Max Planck Inst Biochem, Abt Strukturforsch, D-82152 Martinsried, Germany
Tech Univ Munich, Lehrstuhl Organ Chem & Biochem, D-85747 Garching, Germany
Russian Acad Sci, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bauer, S...; Schott, A.K.; Illarionova, V...; Bacher, A...; Huber, R...; Fischer, M...

Найти похожие

The possible way of introducing mineral elements of liquid human wastes into the material cycle in biological life support systems / A. A. Tikhomirov [et al.] // International Astronautical Federation - 55th International Astronautical Congress 2004. - 2004. - Vol. 3: International Astronautical Federation - 55th International Astronautical Congress 2004 (4 October 2004 through 8 October 2004, Vancouver) Conference code: 69653. - P1442-1448
Кл.слова (ненормированные):
Biomass -- Body fluids -- Hydrogen peroxide -- Life support systems (spacecraft) -- Solid wastes -- Biological life support systems -- Intrasystem material cycle -- Liquid human wastes -- Plant biomass -- Waste management
Аннотация: Along with the atmosphere, water and food regeneration processes in biological life support systems it is important to provide units and links responsible for utilization of unused plant biomass, human wastes and returning, if possible, the most of wastes into the intrasystem material cycle. The experience on construction of biological life support systems (BLSS) gained by the Institute of Biophysics SB RAS (Krasnoyarsk, Russia) allows us to suggest constructing an integrated biological-physical-chemical life support system with the biological unit predominating. It is possibly to partially mineralize urine and solid wastes by "wet incineration" by hydrogen peroxide in electric field. We suggest decomposing urea by a urease-enzymatic method using soybean or canavalia flour containing sufficient amount of urease. Consumption of 1.5 g of flour for decomposition of urea in daily urine and the possibility of producing flour from soybeans and canavalia grown inside the system make this method of urea decomposition rather prospective. Further ammonia distillation using the nitrification unit and evaporation of solution would make possible to return nitrogen and water back into the intrasystem cycle. Probably, in long-duration space expeditions the utilization of urine would be confined only by extraction of nitrogen and water from urine with further removal of dry residue to the stock, as the problem of returning sodium chloride into the intrasystem cycling has not been solved yet. As all biogenic elements contained in urine (except nitrogen) get lost at that, the solution of the problem with introducing NaCl and mineral elements into the cycle with the help of halophyte plants Salicornia europaea are of sufficient interest. This work presents the experimental results of growing Salicornia europaea on model solutions containing biogenic elements in the amounts equivalent to their content in urine and on urine, which undergone physically-chemically treatment by peroxide and ammonia distillation after urease-enzymatic decomposition. Taking into consideration that the mineral elements content in urine can vary, 2 variants of model solutions were used. In the first variant the content of P was 8-fold, S - 7-fold, K - 8-fold higher than in Knop's solution; the content of Ca and Mg almost complied with that in Knop's solution. In the variant P was 12-fold, S - 17-fold, K - 17-fold, Ca - 6-fold and Mg was 8-fold higher than in Knop's solution. The content of N and NaCl in both variants was the same and constituted 0.18 g/l and 10 g/l respectively. The results of carried experiments showed that growing plants on urine treated in the above-mentioned way is possible; though the productivity of plants would be less than on model solutions. The reasons of plant productivity drop and the possible ways of their removal have been discussed.

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

Доп.точки доступа:
Tikhomirov, A.A.; Gitelson, J.I.; Ushakova, S.A.; Kovaleva, N.P.; Tikhomirova, N.A.; Gribovskaya, I.V.

Найти похожие

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.

Найти похожие

Application of Enzyme Bioluminescence in Ecology [Text] / E. Esimbekova, V. Kratasyuk, O. Shimomura // Adv. Biochem. Eng. Biotechnol. : SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - P67-109. - (Advances in Biochemical Engineering-Biotechnology), DOI 10.1007/978-3-662-43385-0_3. - Cited References:85 . -

РУБ Biotechnology & Applied Microbiology
Рубрики:
BACTERIAL LUCIFERASE
   IN-VITRO
   PYRETHROID INSECTICIDES
   FRESH-WATER
Кл.слова (ненормированные):
Bioluminescence -- Ecological monitoring -- Enzymatic assay -- Immobilization -- Integral water toxicity -- Luciferase
Аннотация: This review examines the general principles of bioluminescent enzymatic toxicity bioassays and describes the applications of these methods and the implementation in commercial biosensors. Bioluminescent enzyme system technology (BEST) has been proposed in the bacterial coupled enzyme system, wherein NADH: FMN-oxidoreductase-luciferase substitutes for living organisms. BEST was introduced to facilitate and accelerate the development of cost-competitive enzymatic systems for use in biosensors for medical, environmental, and industrial applications. For widespread use of BEST, the multicomponent reagent "Enzymolum'' has been developed, which contains the bacterial luciferase, NADH: FMN-oxidoreductase, and their substrates, co-immobilized in starch or gelatin gel. Enzymolum is the central part of Portable Laboratory for Toxicity Detection (PLTD), which consists of a biodetector module, a sampling module, a sample preparation module, and a reagent module. PLTD instantly signals chemical-biological hazards and allows us to detect a wide range of toxic substances. Enzymolum can be integrated as a biological module into the portable biodetector-biosensor originally constructed for personal use. Based on the example of Enzymolum and the algorithm for creating new enzyme biotests with tailored characteristics, a new approach was demonstrated in biotechnological design and construction. The examples of biotechnological design of various bioluminescent methods for ecological monitoring were provided. Possible applications of enzyme bioassays are seen in the examples for medical diagnostics, assessment of the effect of physical load on sportsmen, analysis of food additives, and in practical courses for higher educational institutions and schools. The advantages of enzymatic assays are their rapidity (the period of time required does not exceed 3-5 min), high sensitivity, simplicity and safety of procedure, and possibility of automation of ecological monitoring; the required luminometer is easily available.

WOS
Держатели документа:
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ИБФ СО РАН

Доп.точки доступа:
Esimbekova, Elena; Kratasyuk, Valentina; Shimomura, Osamu

Найти похожие

10.

Bioluminescent Enzymatic Methods for Toxicological Safety Testing of Food Additives [Text] / A. . Asanova, E. . Esimbekova, V. . Kratasyuk // Luminescence. - 2014. - Vol. 29. - P74-74. - Cited References: 4 . - ISSN 1522-7235. - ISSN 1522-7243
Рубрики:
ASSAY

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

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

Найти похожие

11.

Application of bioluminescent enzymatic method for assessment of the state of the soil [Text] / N. . Rimatskaia [et al.] // Luminescence. - 2014. - Vol. 29. - P76-77. - Cited References: 0 . - ISSN 1522-7235. - ISSN 1522-7243

WOS
Держатели документа:
[Rimatskaia, Nadezhda
Baigina, Elizaveta
Kazanceva, Marina
Kratasyuk, Valentina] Siberian Fed Univ, Krasnoyarsk, Russia
[Kratasyuk, Valentina] Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk, Russia
[Stom, Devard] Irkutsk State Univ, Irkutsk 664003, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Rimatskaia, N...; Baigina, E...; Kazanceva, M...; Stom, D...; Kratasyuk, V...

Найти похожие

12.

Applications of Luminous Bacteria Enzymes in Toxicology [Text] / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959, DOI 10.2174/1386207318666150917100257. - Cited References:88. - The research was supported by the Russian Science Foundation, project No. 15-19-10041. . - ISSN 1386-2073. - ISSN 1875-5402

РУБ Biochemical Research Methods + Chemistry, Applied + Pharmacology &
Рубрики:
NADHFMN-OXIDOREDUCTASE-LUCIFERASE
HUMIC SUBSTANCES
BIOLUMINESCENT
Кл.слова (ненормированные):
Bioluminescence -- bioluminescent toxicity enzymatic assay -- immobilization -- of enzymes -- luciferase -- total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH: FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Esimbekova, Elena N.; Russian Science Foundation [15-19-10041]

Найти похожие

13.

Applications of luminous bacteria enzymes in toxicology / V. A. Kratasyuk, E. N. Esimbekova // Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - P952-959 . - ISSN 1386-2073
Кл.слова (ненормированные):
Bioluminescence -- Bioluminescent toxicity enzymatic assay -- Immobilization of enzymes -- Luciferase -- Total toxicity
Аннотация: This review describes the principle and applications of bioluminescent enzymatic toxicity bioassays. This type of assays uses bacterial coupled enzyme systems: NADH:FMN-oxidoreductase and luciferase to replace living organisms in developing cost-competitive biosensors for environmental, medical and industrial applications. These biosensors instantly signal chemical and biological hazards and allow for detecting a great amount of toxic compounds with advantages associated with fast results, high sensitivity, simplicity, low cost and safety of the procedure. © 2015 Bentham Science Publishers.

Scopus
Держатели документа:
Siberian Federal University, Svobodnii Ave., 79, Krasnoyarsk, Russian Federation
Photobiology Laboratory, Russian Academy of Sciences, Siberian Branch, Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, Russian Federation

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

Найти похожие

14.

Design of multicomponent reagents for enzymatic assays [Text] / E. N. Esimbekova [et al.] // Dokl. Biochem. Biophys. - 2015. - Vol. 461, Is. 1. - P102-105, DOI 10.1134/S1607672915020106. - Cited References:8. - The work was supported by the Program of the Russian Academy of Sciences "Molecular and Cell Biology" (project no. 6.8) as well as within the state contract between the Ministry of Education and Science of the Russian Federation and Siberian Federal University (project 1762). . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
BIOLUMINESCENT
WATER

WOS
Держатели документа:
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Esimbekova, E. N.; Lonshakova-Mukina, V. I.; Bezrukikh, A. E.; Kratasyuk, V. A.; Program of the Russian Academy of Sciences "Molecular and Cell Biology" [6.8]; Ministry of Education and Science of the Russian Federation; Siberian Federal University [1762]

Найти похожие

15.

Pollutant toxicity and detoxification by humic substances: mechanisms and quantitative assessment via luminescent biomonitoring [Text] / N. S. Kudryasheva, A. S. Tarasova // Environ. Sci. Pollut. Res. - 2015. - Vol. 22, Is. 1. - P155-167, DOI 10.1007/s11356-014-3459-6. - Cited References:120. - The work was supported by the Russian Foundation for Basic Research,Grant No. 13-04-98072-sibir-a. Part of the work (analysis ofdetoxification of radioactive solutions) was supported by the RussianScience Foundation, Grant No. 14-14-00076. . - ISSN 0944-1344. - ISSN 1614-7499

РУБ Environmental Sciences
Рубрики:
PHOTOBACTERIUM-LEIOGNATHI LUCIFERASE
DISSOLVED ORGANIC-MATTER
Кл.слова (ненормированные):
Detoxification mechanisms -- Humic substances -- Pollutants -- Bioassays -- Bioluminescence
Аннотация: The paper considers mechanisms of detoxification of pollutant solutions by water-soluble humic substances (HSs), natural detoxifying agents. The problems and perspectives of bioassay application for toxicity monitoring of complex solutions are discussed from ecological point of view. Bioluminescence assays based on marine bacteria and their enzymes are of special attention here; they were shown to be convenient tools to study the detoxifying effects on cellular and biochemical levels. The advantages of bioluminescent enzymatic assay for monitoring both integral and oxidative toxicities in complex solutions of model pollutants and HS were demonstrated. The efficiencies of detoxification of the solutions of organic oxidizers and salts of metals (including radioactive ones) by HS were analyzed. The dependencies of detoxification efficiency on time of exposure to HS and HS concentrations were demonstrated. Antioxidant properties of HS were considered in detail. The detoxifying effects of HS were shown to be complex and regarded as 'external' (binding and redox processes in solutions outside the organisms) and/or 'internal' organismal processes. The paper demonstrates that the HS can stimulate a protective response of bacterial cells as a result of (1) changes of rates of biochemical reactions and (2) stabilization of mucous layers outside the cell walls. Acceleration of auto-oxidation of NADH, endogenous reducer, by HS was suggested as a reason for toxicity increase in the presence of HS due to abatement of reduction ability of intracellular media.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
RAS, Inst Biophys, SB, Krasnoyarsk 660036, Russia.
ИБФ СО РАН

Доп.точки доступа:
Kudryasheva, N.S.; Tarasova, A.S.; Russian Foundation for Basic Research [13-04-98072-sibir-a]; RussianScience Foundation [14-14-00076]

Найти похожие

16.

Antioxidant activity of humic substances via bioluminescent monitoring in vitro [Text] / A. S. Tarasova, D. I. Stom, N. S. Kudryasheva // Environ. Monit. Assess. - 2015. - Vol. 187, Is. 3. - Ст. 89, DOI 10.1007/s10661-015-4304-1. - Cited References:51. - This work was supported by the Russian Foundation for Basic Research, Grant No. 15-03-06786a, the Program "Molecular and Cellular Biology" of the Russian Academy of Sciences, project VI 57.1.1. . - ISSN 0167-6369. - ISSN 1573-2959

РУБ Environmental Sciences
Рубрики:
DETOXIFICATION PROCESSES
   TOXICITY
   BIOASSAYS
   BACTERIA
   ASSAY
Кл.слова (ненормированные):
Antioxidant activity -- Oxidative toxicity -- General toxicity -- Humic -- substances -- Bioassay -- Bioluminescence
Аннотация: This work considers antioxidant properties of natural detoxifying agents-humic substances (HS) in solutions of model inorganic and organic compounds of oxidative nature-complex salt K-3[Fe(CN)(6)] and 1,4-benzoquinone. Bioluminescent system of coupled enzymatic reactions catalyzed by NAD(P) H:FMN-oxidoreductase and bacterial luciferase was used as a bioassay in vitro to monitor toxicity of the oxidizer solutions. Toxicities of general and oxidative types were evaluated using bioluminescent kinetic parameters-bioluminescence intensity and induction period, respectively. Antioxidant activity of HS was attributed to their ability to decrease both general and oxidative toxicities; the HS antioxidant efficiency was characterized with detoxification coefficients D-GT and D-OxT, respectively. Dependencies of D-GT and D-OxT on HS concentration and time of preliminary incubation of the oxidizers with HS were demonstrated. The optimal conditions for detoxification of the oxidizers were >20-min incubation time and 0.5x10(-4) to 2x10(-4) M of HS concentration. The present study promotes application of the enzymatic luminescent bioassay to monitor toxicity of pollutants of oxidative nature in environmental and waste waters in remediation procedures.

WOS
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Irkutsk State Univ, Irkutsk 664003, Russia.
ИБФ СО РАН

Доп.точки доступа:
Tarasova, A.S.; Stom, D.I.; Kudryasheva, N.S.; Russian Foundation for Basic Research [15-03-06786a]; Russian Academy of Sciences [VI 57.1.1]

Найти похожие

17.

Structural distinctions of fast and slow bacterial luciferases revealed by phylogenetic analysis [Text] / A. A. Deeva [et al.] // Bioinformatics. - 2016. - Vol. 32, Is. 20. - P3053-3057, DOI 10.1093/bioinformatics/btw386. - Cited References:31. - The reported study was partially funded by RFBR according to the research project No. 16-34-00746 mol_a; by the Ministry of Education and Science of the Russian Federation [project No 1762] and by the state budget allocated to the fundamental research at the Russian Academy of Sciences [project No 01201351504]. . - ISSN 1367-4803. - ISSN 1460-2059

РУБ Biochemical Research Methods + Biotechnology & Applied Microbiology

Аннотация: Motivation: Bacterial luciferases are heterodimeric enzymes that catalyze a chemical reaction, so called bioluminescence, which causes light emission in bacteria. Bioluminescence is vastly used as a reporter system in research tools and commercial developments. However, the details of the mechanisms that stabilize and transform the reaction intermediates as well as differences in the enzymatic kinetics amongst different bacterial luciferases remain to be elucidated. Results: Amino acid sequences alignments for 21 bacterial luciferases (both alpha- and beta-subunits) were analyzed. For alpha-subunit, containing the enzyme active center, 48 polymorphic amino acid positions were identified. According to them, the sequences fell into two distinct groups known as slow and fast based on the decay rate of the bioluminescence reaction. The differences in the enzyme active site induced by structural polymorphism are analyzed.

WOS,
Смотреть статью,
Scopus
Держатели документа:
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk, Russia.
Inst Cell Biophys RAS, Mech Cell Genome Functioning Lab, Pushchino, Moscow Region, Russia.
Moscow Inst Phys & Technol, Dolgoprudnyi, Russia.
Inst Biophys SB RAS, Lab Photobiol, Krasnoyarsk, Russia.

Доп.точки доступа:
Deeva, Anna A.; Temlyakova, Evgenia A.; Sorokin, Anatoly A.; Nemtseva, Elena V.; Kratasyuk, Valentina A.; RFBR [16-34-00746 mol_a]; Ministry of Education and Science of the Russian Federation [1762]; state budget allocated to the fundamental research at Russian Academy of Sciences [01201351504]

Найти похожие

18.

The disulfide-rich Metridia luciferase refolded from E. coli inclusion bodies reveals the properties of a native folded enzyme produced in insect cells / S. V. Markova [et al.] // J. Photochem. Photobiol. B-Biol. - 2017. - Vol. 175. - P51-57, DOI 10.1016/j.jphotobiol.2017.08.024. - Cited References:30. - These studies were funded by RFBR and the Government of Krasnoyarsk Territory according to the research project No. 16-44-242099 and the state budget allocated to the fundamental research at the Russian Academy of Sciences (project No. 0356-2016-0712). . - ISSN 1011-1344

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
GAUSSIA-PRINCEPS LUCIFERASE
   ESCHERICHIA-COLI
   EXPRESSION
   PROTEIN
Кл.слова (ненормированные):
Copepod luciferase -- Disulfide bonds -- Cysteine-rich protein -- Oxidative -- refolding
Аннотация: The bioluminescence of a marine copepod Metridia Tonga is determined by a small secreted coelenterazine-dependent luciferase that uses coelenterazine as a substrate of enzymatic reaction to generate light (lambda(max) = 480 nm). To date, four different isoforms of the luciferase differing in size, sequences, and properties have been cloned by functional screening. All of them contain ten conserved Cys residues that suggests up to five S-S intramolecular bonds per luciferase molecule. Whereas the use of copepod luciferases as bioluminescent reporters in biomedical research in vivo is growing from year to year, their application for in vitro assays is still limited by the difficulty in obtaining significant amounts of luciferase. The most cost-effective host for producing recombinant proteins is Escherichia coli. However, prokaryotic and eukaryotic cells maintain the reductive environment in cytoplasm that hinders the disulfide bond formation and consequently the proper folding of luciferase. Here we report the expression of the MLuc7 isoform of M. longa luciferase in E. colt cells and the efficient procedure for refolding from inclusion bodies yielding a high-active monomeric protein. Furthermore, in a set of identical experiments we demonstrate that bioluminescent and structural features of MLuc7 produced in bacterial cells are identical to those of MLuc7 isoform produced from culture medium of insect cells. Although the yield of high-purity protein is only 6 mg/L, the application of E. coil cells to produce the luciferase is simpler and more cost-effective than the use of insect cells. We expect that the suggested technology of Metridia luciferase production allows obtaining of sufficient amounts of protein both for the development of novel in vitro analytical assays with the use of MLuc7 as a label and for structural studies.

WOS,
Смотреть статью
Держатели документа:
RAS, Krasnoyarsk Sci Ctr SB, Fed Res Ctr, Photobiol Lab,Inst Biophys SB, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

Доп.точки доступа:
Markova, Svetlana V.; Larionova, Marina D.; Gorbunova, Darya A.; Vysotski, Eugene S.; RFBR; Government of Krasnoyarsk Territory [16-44-242099]; Russian Academy of Sciences [0356-2016-0712]

Найти похожие

19.

Antioxidant Activity of Fullerenols. Bioluminescent Monitoring in vitro / A. S. Sachkova [et al.] ; ed.: A. . Turner, A. . Tang // BIOSENSORS 2016 : ELSEVIER SCIENCE BV, 2017. - Vol. 27: 26th Anniversary World Congress on Biosensors (Biosensors) (MAY 25-27, 2016, Gothenburg, SWEDEN). - P230-231. - (Procedia Technology), DOI 10.1016/j.protcy.2017.04.097. - Cited References:2. - The work was supported by the Russian Foundation for Basic Research, Grants No. 15-03-06786 and 15-43-04377-sibir; the state budget to the fundamental research at the Russian Academy of Sciences (project No 01201351504) . -

РУБ Engineering, Biomedical

Кл.слова (ненормированные):
bioluminescence -- enzymatic assay -- toxicity sensor -- antioxidant activity -- fullerenol
Аннотация: Bioluminescence of isolated enzymes is a perspective phenomenon for biosensors development due to simplicity of registration of a physiological parameter - light intensity. Enzyme-based bioluminescent assay is widely used to evaluate a decrease in biochemical toxicities. Also the enzyme-based assay is used for the direct biochemical monitoring of oxidative toxicity. This work considers antioxidant properties of fullerenols, water-soluble polyhydroxylated derivatives of fullerenes and perspective pharmaceutical agents, in solutions of model inorganic and organic toxicants of oxidative type K-3[Fe(CN)(6)] and 1,4-benzoquinone. Two fullerenol preparations were used: C60O2-4(OH)(20-24) and mixture of two types of fullerenols C60O2-4(OH)(20-24)+C70O2-4(OH)(20-24). The enzyme-based assays showed the peculiarities of the detoxification processes: ultralow concentrations of fullerenols were active (ca 10(-17)-10(-5)g/L); no monotonic dependence of detoxification efficiency on fullerenol concentrations was observed, and detoxification of organic oxidizer solutions was more effective than that of the inorganic oxidizer. The antioxidant effects of highly diluted fullerenol solutions were attributed to hormesis phenomenon; the detoxification was concerned with stimulation of adaptive cellular response under low-dose exposures. (C) 2017 The Authors. Published by Elsevier Ltd.

WOS,
Смотреть статью
Держатели документа:
Natl Res Tomsk Polytech Univ, Lenin Ave 30, Tomsk 634050, Russia.
SB RAS, Inst Biophys, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Svobodny Pr 79, Krasnoyarsk 660041, Russia.

Доп.точки доступа:
Sachkova, A. S.; Kovel, E. S.; Vorobeva, A. A.; Kudryasheva, N. S.; Turner, A... \ed.\; Tang, A... \ed.\; Russian Foundation for Basic Research [15-03-06786, 15-43-04377-sibir]; state budget to the fundamental research at the Russian Academy of Sciences [01201351504]

Найти похожие

20.

Analytical Enzymatic Reactions in Microfluidic Chips / K. A. Lukyanenko [et al.] // Appl. Biochem. Microbiol. - 2017. - Vol. 53, Is. 7. - P775-780, DOI 10.1134/S0003683817070043. - Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041). . - ISSN 0003-6838. - ISSN 1573-8183

РУБ Biotechnology & Applied Microbiology + Microbiology
Рубрики:
BIOAVAILABLE HEAVY-METALS
   DEVICES
   POINT
   LAB
Кл.слова (ненормированные):
bioluminescence -- luciferase -- microfluidics -- microfluidic chip -- enzymatic -- bioassay
Аннотация: A number of approaches have been proposed and tested to transfer enzymatic reactions into the functional elements of microfluidic chips on the example of the bienzyme bioluminescent reaction involving NAD(P)H:FMN-oxidoreductase and luciferase. Measurement of the catalytic activity of these enzymes (under the influence of pollutants) is the basis of enzymatic bioassay of various liquids. It was found that all of the components of the reaction must be placed in the same cell of the chip to improve the reproducibility of the measurements. The use of starch gel as a carrier for immobilization and gelatin as a scaffold in the reactor of the chip enables the preservation of enzyme activity in the course of sealing the chip at room temperature. It is shown that the components of the reaction should be vigorously stirred in a microfluidic chip reactor to improve the efficiency of the analysis. As a result of the studies, a prototype of microfluidic chip based on the enzymatic bioluminescent reaction is proposed. It is characterized by a detection limit of copper sulfate of 3 mu M that corresponds to the sensitivity of traditional lux-biosensors based on living cells. The analysis time is reduced to 1 min, and the analysis can be performed by individuals without special laboratory skills.

WOS,
Смотреть статью,
Scopus
Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia.
St Petersburg Inst Fine Mech & Opt, St Petersburg 197101, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, K. A.; Denisov, I. A.; Yakimov, A. S.; Esimbekova, E. N.; Belousov, K. I.; Bukatin, A. S.; Kukhtevich, I. V.; Sorokin, V. V.; Evstrapov, A. A.; Belobrov, P. I.; Russian Science Foundation [15-19-10041]

Найти похожие