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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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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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A database on natural and transgenic luminous microorganisms: BiolumBase / S. E. Medvedeva [et al.] // Microbiology. - 2005. - Vol. 74, Is. 2. - P236-243, DOI 10.1007/s11021-005-0057-0 . - ISSN 0026-2617
Кл.слова (ненормированные):
Bioluminescence -- Database -- Natural and transgenic luminous microorganisms -- Bacteria (microorganisms)
Аннотация: The database BiolumBase was designed for the collection and systematization of available information on microorganisms containing bioluminescent systems; it includes two sections: natural and transgenic luminous microorganisms. By now, logic schemes of these sections have been developed, classification of the objects has been performed, ways of presentation of characteristics and structure of fields for input of information have been elaborated, and the necessary program modules have been developed. The database is filled on the basis of published data and our own experimental results; subsequent linkage of the database to the Internet is envisaged. Users will be able to obtain not only catalogues of strains but also information concerning the properties and functions of the known species of luminous bacteria, the structure, regulatory mechanisms, and application of bioluminescent systems and genetically engineered constructions with lux genes, as well as to find references and to search strains by using any set of attributes. The database will provide information that is of interest for the development of microbial ecology and biotechnology, in particular, for the prediction of biological hazard from the application of transgenic strains. В© 2005 Pleiades Publishing, Inc.

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

Доп.точки доступа:
Medvedeva, S.E.; Boyandin, A.N.; Lankin, Yu.P.; Kotov, D.A.; Kargatova, T.V.; Rodicheva, E.K.; Popova, L.Yu.

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A GEL MODEL FOR THE FUNCTIONING OF LUCIFERASE IN THE CELL [Text] / V. A. KRATASYUK, V. V. ABAKUMOVA, N. B. KIM // Biochem.-Moscow. - 1994. - Vol. 59, Is. 7. - P. 761-765. - Cited References: 11 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
BIOLUMINESCENT
Кл.слова (ненормированные):
BIOLUMINESCENCE -- LUCIFERASE -- NADH, FMN-OXIDOREDUCTASE -- IMMOBILIZATION
Аннотация: A gel model for the functioning of luciferase in cells has been constructed using bacterial NADH:FMN-oxidoreductase and luciferase immobilized in starch gel disks. The characteristics of the immobilized luciferase depend on the duration of drying, the amount and concentration of the gel, the nature of the support used for drying, and the properties of the initial enzyme preparation. Functionally important enzyme groups remain intact in the immobilized preparation, and luciferase retains its high specificity with respect to aldehydes. The gel microenvironment appears to be optimal for luciferase, judging from its high activity and increased stability. Conditions allowing repeated use of the preparation have been found. The approach permits co-immobilization of luciferase with other enzymes and their substrates. The error in bioluminescence measurements using the disks is 5-10%. A procedure for stabilization of the immobilized luciferase during repeated use has been devised.

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

Доп.точки доступа:
KRATASYUK, V.A.; ABAKUMOVA, V.V.; KIM, N.B.

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A noninvasive and qualitative bioluminescent assay for express diagnostics of athletes' responses to physical exertion / V. A. Kratasyuk, L. V. Stepanova, R. Ranjan [et al.] // Luminescence. - 2020, DOI 10.1002/bio.3954. - Cited References:33. - The Ministry of Science and Higher Education of the Russian Federation, Grant/Award Number: FSRZ-2020-0006; Krasnoyarsk Regional Foundation of Science, Grant/Award Number: KF-537 . - Article in press. - ISSN 1522-7235. - ISSN 1522-7243

РУБ Chemistry, Analytical
Рубрики:
SALIVARY BIOMARKERS
EXERCISE
Кл.слова (ненормированные):
athletes -- BLuc‐ -- Red coupled enzyme system -- catalase activity -- saliva -- training load
Аннотация: Upcoming professional sports authorities seek rapid noninvasive biosensing tools for regular monitoring of athletes' physiological states. The analysis of saliva through luminescence-based biosensors has been perceived as a suitable candidate for such purposes. The present study reports a qualitative bioluminescence assay based on a coupled enzyme system that consists of bacterial luciferase (BLuc) and nicotinamide adenine dinucleotide (NADH):flavin mononucleotide (FMN) oxidoreductase (Red), BLuc-Red, for the express diagnostics of athletes' stress levels before and after physical exertion. The volunteers who participated in the study were grouped as freestyle wrestlers and students who adapted to different levels of physical activities. Under physical exertion modelling conditions, the influence of participant saliva on BLuc-Red catalyzed light emission was investigated. Results showed a significant increase in residual luminescence (I-exp, mean maximum bioluminescence intensity of the experimental measurement (I-exp); I-c, luminescence intensity in control; I-exp/I-c, %) values for participants in the wrestler group while a decrease in the student group (P < 0.05). Such contrasting residual luminescence values in both groups were found to be dependent on the catalase activity of saliva. The proposed bioluminescence assay can be utilized as a potential nonspecific biosensing tool for determining the physical state of athletes under high loads.

WOS
Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Dept Biophys, Svobodny Prospect 79, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Akademgorodok 50-50, Akademgorodok, Russia.
Krasnoyarsk State Med Univ, Minist Hlth Russian Federat, Av Partizan Zheleznyak 1, Krasnoyarsk, Russia.
Krasnoyarsk Matern & Childhood Protect Ctr, Kirenskogo St 2a, Krasnoyarsk, Russia.
Siberian Fed Univ, Sch Nonferrous Met & Mat Sci, Svobodny Prospect 79, Krasnoyarsk, Russia.
Sci Res Inst Med Problems North, Av Partizan Zheleznyak 3g, Krasnoyarsk, Russia.

Доп.точки доступа:
Kratasyuk, Valentina A.; Stepanova, Lyudmila, V; Ranjan, Rajeev; Sutormin, Oleg S.; Pande, Shubhra; Zhukova, Galina, V; Miller, Olga M.; Maznyak, Natalya, V; Kolenchukova, Oksana A.; Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; Krasnoyarsk Regional Foundation of Science [KF-537]

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A Novel Type of Luciferin from the Siberian Luminous Earthworm Fridericia heliota: Structure Elucidation by Spectral Studies and Total Synthesis [Text] / V. N. Petushkov [et al.] // Angew. Chem.-Int. Edit. - 2014. - Vol. 53, Is. 22. - P5566-5568, DOI 10.1002/anie.201400529. - Cited References: 13. - We thank Dr. Alexander O. Chizhov for recording mass spectra and Dr. K. S. Mineev for NMR analysis of synthetic intermediates. We acknowledge support from the Program of the Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11. G34.31.0058), the programs MCB RAS, President of the Russian Federation "Leading science school" (grant 3951.2012.4) and the Russian Foundation for Basic Research (grant 14-03-01015). B. M. S. was supported by a stipend from the Program of the President of the Russian Federation. . - ISSN 1433-7851. - ISSN 1521-3773

РУБ Chemistry, Multidisciplinary
Рубрики:
BIOLUMINESCENT EARTHWORM
Кл.слова (ненормированные):
bioluminescence -- luciferin -- natural products -- NMR spectroscopy -- total synthesis
Аннотация: The structure elucidation and synthesis of the luciferin from the recently discovered luminous earthworm Fridericia heliota is reported. This luciferin is a key component of a novel ATP-dependent bioluminescence system. UV, fluorescence, NMR, and HRMS spectroscopy studies were performed on 0.005 mg of the isolated substance and revealed four isomeric structures that conform to spectral data. These isomers were chemically synthesized and one of them was found to produce light when reacted with a protein extract from F. heliota. The novel luciferin was found to have an unusual extensively modified peptidic nature, thus implying an unprecedented mechanism of action.

WOS
Держатели документа:
[Petushkov, Valentin N.
Rodionova, Natalja S.
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Petushkov, Valentin N.
Rodionova, Natalja S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Lab Photobiol, Krasnoyarsk 660036, Russia
[Dubinnyi, Maxim A.
Tsarkova, Aleksandra S.
Baranov, Mikhail S.
Kublitski, Vadim S.
Yampolsky, Ilia V.] Russian Acad Sci, Inst Bioorgan Chem, Moscow 117997, Russia
[Shimomura, Osamu] Marine Biol Lab, Woods Hole, MA 02543 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Dubinnyi, M.A.; Tsarkova, A.S.; Rodionova, N.S.; Baranov, M.S.; Kublitski, V.S.; Shimomura, O...; Yampolsky, I.V.; Government of the Russian Federation "Measures to attract leading scientists to Russian educational institutions" [11. G34.31.0058]; programs MCB RAS; Russian Federation "Leading science school" [3951.2012.4]; Russian Foundation for Basic Research [14-03-01015]; Russian Federation

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A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN [Text] / L. Y. Antipina [et al.] // J. Struct. Chem. - 2011. - Vol. 52, Is. 5. - P870-875. - Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213). . - ISSN 0022-4766

РУБ Chemistry, Inorganic & Nuclear + Chemistry, Physical
Рубрики:
CALCIUM-DISCHARGED OBELIN
   SEMIEMPIRICAL METHODS
   1.7 ANGSTROM
   OPTIMIZATION
   PARAMETERS
   MECHANISM
   FLUORESCENCE
   ELEMENTS
   PROTEIN
   EMITTER
Кл.слова (ненормированные):
coelenterazine -- 2-hydroperoxy-coelenterazine -- Obelia longissima -- Renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.

Держатели документа:
[Antipina, L. Yu
Tomilin, F. N.
Ovchinnikov, S. G.] Russian Acad Sci, LV Kirensky Phys Inst, Siberian Div, Krasnoyarsk, Russia
[Vysotskii, E. S.] Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk, Russia
[Antipina, L. Yu
Ovchinnikov, S. G.] MF Reshetnev Siberian State Aerosp Univ, Krasnoyarsk, Russia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Antipina, L.Y.; Tomilin, F.N.; Vysotskii, E.S.; Ovchinnikov, S.G.

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All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin / L. P. Burakova [et al.] // J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - P57-66, DOI 10.1016/j.jphotobiol.2015.11.012 . - ISSN 1011-1344
Кл.слова (ненормированные):
Aequorin -- Bioluminescence -- Calcium -- Coelenterazine -- Obelin
Аннотация: Light-sensitive photoprotein berovin accounts for a bright bioluminescence of ctenophore Beroe abyssicola. Berovin is functionally identical to the well-studied Ca2+-regulated photoproteins of jellyfish, however in contrast to those it is extremely sensitive to the visible light. Berovin contains three EF-hand Ca2+-binding sites and consequently belongs to a large family of the EF-hand Ca2+-binding proteins. Here we report the spatial structure of apo-berovin with bound Mg2+ determined at 1.75 A. The magnesium ion is found in each functional EF-hand loop of a photoprotein and coordinated by oxygen atoms donated by the side-chain groups of aspartate, carbonyl groups of the peptide backbone, or hydroxyl group of serine with characteristic oxygen-Mg2+ distances. As oxygen supplied by the side-chain of the twelfth residue of all Ca2+-binding loops participates in the magnesium ion coordination, it was suggested that Ca2+-binding loops of berovin belong to the mixed Ca2+/Mg2+ rather than Ca2+-specific type. In addition, we report an effect of physiological concentration of Mg2+ on bioluminescence of berovin (sensitivity to Ca2+, rapid-mixed kinetics, light-sensitivity, thermostability, and apo-berovin conversion into active protein). The different impact of physiological concentration of Mg2+ on berovin bioluminescence as compared to hydromedusan photoproteins was attributed to different affinities of the Ca2 +-binding sites of these photoproteins to Mg2+. © 2015 Elsevier B.V. All rights reserved.

Scopus,
WOS
Держатели документа:
Institute of Molecular and Clinical Medicine, Kunming Medical University, Kunming, China
Photobiology Laboratory, Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Akademgorodok 50, Krasnoyarsk, Russian Federation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Beijing, China
IHuman Institute, ShanghaiTech University, 99 Haike Road, Shanghai, China

Доп.точки доступа:
Burakova, L. P.; Natashin, P. V.; Malikova, N. P.; Niu, F.; Pu, M.; Vysotski, E. S.; Liu, Z.-J.
Свободных экз. нет
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All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin [Text] / L. . Deng [et al.] // Protein Sci. - 2005. - Vol. 14, Is. 3. - P663-675, DOI 10.1110/ps.041142905. - Cited References: 46 . - ISSN 0961-8368

РУБ Biochemistry & Molecular Biology
Рубрики:
RAY CRYSTALLOGRAPHIC ANALYSIS
   ANGSTROM RESOLUTION
   SEQUENCE-ANALYSIS
   CA2+-REGULATED PHOTOPROTEINS
   CA2+-DISCHARGED PHOTOPROTEIN
   LUMINESCENT PROTEIN
   MODULATED PROTEINS
   ELECTRON-DENSITY
   CLONING
   CDNA
Кл.слова (ненормированные):
bioluminescence -- EF-hand -- fluorescent protein -- proton relay -- calcium-binding loops -- aequorin -- obelin -- diffraction
Аннотация: The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7 Angstrom and 2.2 Angstrom. respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-proteins retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hydroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with the product, coelenteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these subtle shifts are the basis of the ability of these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.

Держатели документа:
Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
Univ Georgia, Dept Chem, Athens, GA 30602 USA
Russian Acad Sci, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Deng, L...; Vysotski, E.S.; Markova, S.V.; Liu, Z.J.; Lee, J...; Rose, J...; Wang, B.C.

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10.

alpha-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp. / M. A. Dubinnyi, I. A. Ivanov, N. S. Rodionova [et al.] // ChemistrySelect. - 2020. - Vol. 5, Is. 42. - P13155-13159, DOI 10.1002/slct.202003075. - Cited References:49. - This work was supported by the State Assignment for Basic Research of the Russian Academy of Sciences (project no. 0356-2019-0019) and the Russian Foundation for Basic Research (project no. 19-04-00348-a). . - ISSN 2365-6549

РУБ Chemistry, Multidisciplinary
Рубрики:
STRUCTURE ELUCIDATION
   MANNOSYLATION
   TRYPTOPHAN
   PROTEIN
   COMPLEMENT
Кл.слова (ненормированные):
Bioluminescence -- Earthworm -- Henlea -- Natural products -- NMR spectroscopy
Аннотация: Cold extract from bioluminescent earthworm Henlea sp. was studied by HPLC, 1D and 2D NMR and LC-HRMS analysis. An abundant structural analog of the luciferin was isolated and identified as alpha-C-mannosyltryptophan (ManTrp), the product of unusual C2-glycosylation found earlier in humans, ascidians and other animals. Two compounds in cold extract (P300b, P300c) were characterized as C2-substituted derivatives of tryptophan. We hypothesize that a series of tryptophan-containing compounds are possible participants of bioluminescence-related metabolism in Henlea sp.

WOS
Держатели документа:
Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, GSP-7,Miklukho Maklaya Str 16-10, Moscow 117997, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Res Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Pirogov Russian Natl Res Med Univ, 1 Ostrovityanova St, Moscow 117997, Russia.

Доп.точки доступа:
Dubinnyi, Maxim A.; Ivanov, Igor A.; Rodionova, Natalia S.; Kovalchuk, Sergey I.; Kaskova, Zinaida M.; Petushkov, Valentin N.; State Assignment for Basic Research of the Russian Academy of Sciences [0356-2019-0019]; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [19-04-00348-a]

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11.

Analysis of river water by bioluminescent biotests / A. M. Kuznetsov, E. K. Rodicheva, S. E. Medvedeva // Luminescence. - 1999. - Vol. 14, Is. 5. - P263-265 . - ISSN 1522-7235
Кл.слова (ненормированные):
Bioluminescent bioassay -- Pollution -- Water quality -- fresh water -- article -- bioassay -- Escherichia coli -- freeze drying -- genetic procedures -- luminescence -- methodology -- Photobacterium -- Russian Federation -- sensitivity and specificity -- water pollutant -- Biological Assay -- Biosensing Techniques -- Escherichia coli -- Freeze Drying -- Fresh Water -- Luminescence -- Photobacterium -- Russia -- Sensitivity and Specificity -- Water Pollutants, Chemical
Аннотация: The bacterial bioluminescence has high sensitivity to the action of various inhibitors of biological activity. The lyophilized luminous bacteria Photobacterium phosphoreum (Microbiosensor B17 677F) and luminous strain Escherichia coli (Microbiosensor EC) from the Culture Collection IBSO were used to create bioluminescent biotests. They have been applied in ecological monitoring to determine the overall toxicity of the Yenisei and Angara Rivers and some water sources of Altai Territory. As a rule the heaviest pollution of water in studied rivers was registered near cities and settlements. The luminous bacteria biotests are simple and convenient in work, standardized and quantitative, have rapid response to actions of different substances and high sensitivity to environmental pollutants. It takes less than 30 min to do the biotest (the other biotests take 48-96 h). Copyright В© 1999 John Wiley & Sons, Ltd.

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

Доп.точки доступа:
Kuznetsov, A.M.; Rodicheva, E.K.; Medvedeva, S.E.

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12.

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]

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13.

Antioxidant Activity and Toxicity of Fullerenols via Bioluminescence Signaling: Role of Oxygen Substituents / E. S. Kovel [et al.] // Int J Mol Sci. - 2019. - Vol. 20, Is. 9, DOI 10.3390/ijms20092324 . - ISSN 1422-0067
Кл.слова (ненормированные):
antioxidant activity -- bioactive compound -- bioluminescence bioassay -- fullerenol -- reactive oxygen species -- toxicity
Аннотация: Fullerenols are nanosized water-soluble polyhydroxylated derivatives of fullerenes, a specific allotropic form of carbon, bioactive compounds, and perspective basis for drug development. Our paper analyzes the antioxidant activity and toxicity of a series of fullerenols with different number of oxygen substituents. Two groups of fullerenols were under investigation: (1) C60Oy(OH)x, C60,70Oy(OH)x, where x + y = 24-28 and (2) C60,70Oy(OH)x, Fe0,5C60Oy(OH)x, Gd@C82Oy(OH)x, where x + y = 40-42. Bioluminescent cellular and enzymatic assays (luminous marine bacteria and their enzymatic reactions, respectively) were applied to monitor toxicity in the model fullerenol solutions and bioluminescence was applied as a signaling physiological parameter. The inhibiting concentrations of the fullerenols were determined, revealing the fullerenols' toxic effects. Antioxidant fullerenol' ability was studied in solutions of model oxidizer, 1,4-benzoquinone, and detoxification coefficients of general and oxidative types (DGT and DOxT) were calculated. All fullerenols produced toxic effect at high concentrations (>0.01 g L-1), while their antioxidant activity was demonstrated at low and ultralow concentrations (<0.001 g L-1). Quantitative toxic and antioxidant characteristics of the fullerenols (effective concentrations, concentration ranges, DGT, and DOxT) were found to depend on the number of oxygen substituents. Lower toxicity and higher antioxidant activity were determined in solutions of fullerenols with fewer oxygen substituents (x + y = 24-28). The differences in fullerenol properties were attributed to their catalytic activity due to reversible electron acceptance, radical trapping, and balance of reactive oxygen species in aqueous solutions. The results provide pharmaceutical sciences with a basis for selection of carbon nanoparticles with appropriate toxic and antioxidant characteristics. Based on the results, we recommend, to reduce the toxicity of prospective endohedral gadolinium-fullerenol preparations Gd@C82Oy(OH)x, decreasing the number of oxygen groups to x + y = 24-28. The potential of bioluminescence methods to compare toxic and antioxidant characteristics of carbon nanostructures were demonstrated.

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Держатели документа:
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Institute of Physics SB RAS, Krasnoyarsk, 660036, Russian Federation
National Research Tomsk Polytechnic University, Tomsk, 634050, Russian Federation
Institute of Physics SB RAS, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Kovel, E. S.; Sachkova, A. S.; Vnukova, N. G.; Churilov, G. N.; Knyazeva, E. M.; Kudryasheva, N. S.

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14.

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.

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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]

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15.

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.

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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]

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16.

Application of Enzyme Bioluminescence for Medical Diagnostics [Text] / L. A. Frank, V. V. Krasitskaya // Adv. Biochem. Eng. Biotechnol. : SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - P175-197. - (Advances in Biochemical Engineering-Biotechnology), DOI 10.1007/978-3-662-43385-0_6. - Cited References:63 . -

РУБ Biotechnology & Applied Microbiology
Рубрики:
RESONANCE ENERGY-TRANSFER
POLYMERASE-CHAIN-REACTION
LUCIFERASE
Кл.слова (ненормированные):
Bioluminescence -- Ca2+-regulated photoprotein -- Diagnostics -- Immunoassay -- Luciferase -- Nucleic acid hybridization assay
Аннотация: Nowadays luciferases are effectively used as analytical instruments in a great variety of research fields. Of special interest are the studies dealing with elaboration of novel analytical systems for the purposes of medical diagnostics. The ever-expanding spectrum of clinically important analytes accounts for the increasing demand for new techniques for their detection. In this chapter we have made an attempt to summarize the results on applications of luciferases as reporters in binding assays including immunoassay, nucleic acid hybridization assay, and so on. The data over the last 15 years have been analyzed and clearly show that luciferase-based assays, due to extremely high sensitivity, low cost, and the lack of need for skilled personnel, hold much promise for clinical diagnostics.

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

Доп.точки доступа:
Frank, Ludmila A.; Krasitskaya, Vasilisa V.

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17.

    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

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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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18.

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.

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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

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19.

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]

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20.

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.

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