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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V.A., Egorova O.I., Esimbekova E.N., Kudryashova N.S., Orlova N.Y., L'vova L.S.
Заглавие : A biological luciferase test for the bioluminescent assay of wheat grain infection with Fusarium
Колич.характеристики :3 с
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA, 1998. - Vol. 34, Is. 6. - P622-624. - ISSN 0003-6838
Примечания : Cited References: 7
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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Lesnyak D.V., Popova L.Y.
Заглавие : A conflict: Induction-inhibition of luminescence in the expression of lux-genes in transgenic bacteria
Колич.характеристики :5 с
Место публикации : Biofizika: MEZHDUNARODNAYA KNIGA, 2002. - Vol. 47, Is. 6. - P1059-1063. - ISSN 0006-3029
Примечания : Cited References: 12
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Medvedeva S.E., Boyandin A.N., Lankin Yu.P., Kotov D.A., Kargatova T.V., Rodicheva E.K., Popova L.Yu.
Заглавие : A database on natural and transgenic luminous microorganisms: BiolumBase
Место публикации : Microbiology. - 2005. - Vol. 74, Is. 2. - С. 236-243. - ISSN 00262617 (ISSN) , DOI 10.1007/s11021-005-0057-0
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : KRATASYUK V.A., ABAKUMOVA V.V., KIM N.B.
Заглавие : A GEL MODEL FOR THE FUNCTIONING OF LUCIFERASE IN THE CELL
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1994. - Vol. 59, Is. 7. - P761-765. - ISSN 0006-2979
Примечания : Cited References: 11
Предметные рубрики: BIOLUMINESCENT
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : 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.
Заглавие : A noninvasive and qualitative bioluminescent assay for express diagnostics of athletes' responses to physical exertion
Колич.характеристики :7 с
Коллективы : Ministry of Science and Higher Education of the Russian Federation [FSRZ-2020-0006]; Krasnoyarsk Regional Foundation of Science [KF-537]
Место публикации : Luminescence: WILEY, 2020. - Article in press. - ISSN 1522-7235, DOI 10.1002/bio.3954. - ISSN 1522-7243(eISSN)
Примечания : 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
Предметные рубрики: SALIVARY BIOMARKERS
EXERCISE
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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Dubinnyi M.A., Tsarkova A.S., Rodionova N.S., Baranov M.S., Kublitski V.S., Shimomura O..., Yampolsky I.V.
Заглавие : A Novel Type of Luciferin from the Siberian Luminous Earthworm Fridericia heliota: Structure Elucidation by Spectral Studies and Total Synthesis
Колич.характеристики :3 с
Коллективы : 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
Место публикации : Angew. Chem.-Int. Edit.: WILEY-V C H VERLAG GMBH, 2014. - Vol. 53, Is. 22. - С. 5566-5568. - ISSN 1433-7851, DOI 10.1002/anie.201400529. - ISSN 1521-3773
Примечания : 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.
Предметные рубрики: BIOLUMINESCENT EARTHWORM
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Antipina L.Y., Tomilin F.N., Vysotskii E.S., Ovchinnikov S.G.
Заглавие : A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN
Колич.характеристики :6 с
Место публикации : J. Struct. Chem.: SPRINGER, 2011. - Vol. 52, Is. 5. - С. 870-875. - ISSN 0022-4766
Примечания : 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).
Предметные рубрики: CALCIUM-DISCHARGED OBELIN
SEMIEMPIRICAL METHODS
1.7 ANGSTROM
OPTIMIZATION
PARAMETERS
MECHANISM
FLUORESCENCE
ELEMENTS
PROTEIN
EMITTER
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Burakova L. P., Natashin P. V., Malikova N. P., Niu F., Pu M., Vysotski E. S., Liu Z.-J.
Заглавие : All Ca2+-binding loops of light-sensitive ctenophore photoprotein berovin bind magnesium ions: The spatial structure of Mg2 +-loaded apo-berovin
Место публикации : J. Photochem. Photobiol. B Biol. - 2016. - Vol. 154. - С. 57-66. - ISSN 10111344 (ISSN) , DOI 10.1016/j.jphotobiol.2015.11.012
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Vysotski E.S., Markova S.V., Liu Z.J., Lee J..., Rose J..., Wang B.C.
Заглавие : All three Ca2+-binding loops of photoproteins bind calcium ions: The crystal structures of calcium-loaded apo-aequorin and apo-obelin
Колич.характеристики :13 с
Место публикации : Protein Sci.: COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, 2005. - Vol. 14, Is. 3. - С. 663-675. - ISSN 0961-8368, DOI 10.1110/ps.041142905
Примечания : Cited References: 46
Предметные рубрики: RAY CRYSTALLOGRAPHIC ANALYSIS
ANGSTROM RESOLUTION
SEQUENCE-ANALYSIS
CA2+-REGULATED PHOTOPROTEINS
CA2+-DISCHARGED PHOTOPROTEIN
LUMINESCENT PROTEIN
MODULATED PROTEINS
ELECTRON-DENSITY
CLONING
CDNA
Ключевые слова (''Своб.индексиров.''): 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.
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10.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Dubinnyi, Maxim A., Ivanov, Igor A., Rodionova, Natalia S., Kovalchuk, Sergey I., Kaskova, Zinaida M., Petushkov, Valentin N.
Заглавие : alpha-C-Mannosyltryptophan is a Structural Analog of the Luciferin from Bioluminescent Siberian Earthworm Henlea sp.
Колич.характеристики :5 с
Коллективы : 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]
Место публикации : ChemistrySelect: WILEY-V C H VERLAG GMBH, 2020. - Vol. 5, Is. 42. - С. 13155-13159. - ISSN 2365-6549, DOI 10.1002/slct.202003075
Примечания : 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).
Предметные рубрики: STRUCTURE ELUCIDATION
MANNOSYLATION
TRYPTOPHAN
PROTEIN
COMPLEMENT
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.
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kuznetsov A.M., Rodicheva E.K., Medvedeva S.E.
Заглавие : Analysis of river water by bioluminescent biotests
Место публикации : Luminescence. - 1999. - Vol. 14, Is. 5. - С. 263-265. - ISSN 15227235 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : 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.
Заглавие : Analytical Enzymatic Reactions in Microfluidic Chips
Колич.характеристики :6 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Appl. Biochem. Microbiol.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2017. - Vol. 53, Is. 7. - С. 775-780. - ISSN 0003-6838, DOI 10.1134/S0003683817070043. - ISSN 1573-8183(eISSN)
Примечания : Cited References:15. - The study was supported by a grant from the Russian Science Foundation (project No. 15-19-10041).
Предметные рубрики: BIOAVAILABLE HEAVY-METALS
DEVICES
POINT
LAB
Ключевые слова (''Своб.индексиров.''): 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.
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kovel E. S., Sachkova A. S., Vnukova N. G., Churilov G. N., Knyazeva E. M., Kudryasheva N. S.
Заглавие : Antioxidant Activity and Toxicity of Fullerenols via Bioluminescence Signaling: Role of Oxygen Substituents
Место публикации : Int J Mol Sci: NLM (Medline), 2019. - Vol. 20, Is. 9. - ISSN 14220067 (ISSN) , DOI 10.3390/ijms20092324
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
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14.

Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Sachkova A. S., Kovel E. S., Vorobeva A. A., Kudryasheva N. S.
Заглавие : Antioxidant Activity of Fullerenols. Bioluminescent Monitoring in vitro
Колич.характеристики :2 с
Коллективы : 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]
Место публикации : BIOSENSORS 2016: ELSEVIER SCIENCE BV, 2017. - Vol. 27: 26th Anniversary World Congress on Biosensors (Biosensors) (MAY 25-27, 2016, Gothenburg, SWEDEN). - С. 230-231. - (Procedia Technology). - , DOI 10.1016/j.protcy.2017.04.097
Примечания : 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)
Ключевые слова (''Своб.индексиров.''): 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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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Tarasova A.S., Stom D.I., Kudryasheva N.S.
Заглавие : Antioxidant activity of humic substances via bioluminescent monitoring in vitro
Колич.характеристики :8 с
Коллективы : Russian Foundation for Basic Research [15-03-06786a], Russian Academy of Sciences [VI 57.1.1]
Место публикации : Environ. Monit. Assess.: SPRINGER, 2015. - Vol. 187, Is. 3. - Ст.89. - ISSN 0167-6369, DOI 10.1007/s10661-015-4304-1. - ISSN 1573-2959(eISSN)
Примечания : 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.
Предметные рубрики: DETOXIFICATION PROCESSES
TOXICITY
BIOASSAYS
BACTERIA
ASSAY
Ключевые слова (''Своб.индексиров.''): 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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16.

Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Frank, Ludmila A., Krasitskaya, Vasilisa V.
Заглавие : Application of Enzyme Bioluminescence for Medical Diagnostics
Колич.характеристики :23 с
Место публикации : Adv. Biochem. Eng. Biotechnol.: SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - С. 175-197. - (Advances in Biochemical Engineering-Biotechnology). - , DOI 10.1007/978-3-662-43385-0_6
Примечания : Cited References:63
Предметные рубрики: RESONANCE ENERGY-TRANSFER
POLYMERASE-CHAIN-REACTION
LUCIFERASE
Ключевые слова (''Своб.индексиров.''): 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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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V..., Esimbekova E...
Заглавие : Application of enzyme bioluminescence in ecology
Колич.характеристики :1 с
Место публикации : Luminescence: WILEY-BLACKWELL, 2014. - Vol. 29. - С. 25-25. - ISSN 1522-7235. - ISSN 1522-7243
Примечания : Cited References: 6
Предметные рубрики: SYSTEM
WATER
ASSAY
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18.

Вид документа : Статья из сборника (выпуск монографической серии)
Шифр издания :
Автор(ы) : Esimbekova, Elena, Kratasyuk, Valentina, Shimomura, Osamu
Заглавие : Application of Enzyme Bioluminescence in Ecology
Колич.характеристики :43 с
Место публикации : Adv. Biochem. Eng. Biotechnol.: SPRINGER-VERLAG BERLIN, 2014. - Vol. 144. - С. 67-109. - (Advances in Biochemical Engineering-Biotechnology). - , DOI 10.1007/978-3-662-43385-0_3
Примечания : Cited References:85
Предметные рубрики: BACTERIAL LUCIFERASE
IN-VITRO
PYRETHROID INSECTICIDES
FRESH-WATER
Ключевые слова (''Своб.индексиров.''): 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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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk, Valentina A., Esimbekova, Elena N.
Заглавие : Applications of Luminous Bacteria Enzymes in Toxicology
Колич.характеристики :8 с
Коллективы : Russian Science Foundation [15-19-10041]
Место публикации : Comb. Chem. High Throughput Screen: BENTHAM SCIENCE PUBL LTD, 2015. - Vol. 18, Is. 10. - С. 952-959. - ISSN 1386-2073, DOI 10.2174/1386207318666150917100257. - ISSN 1875-5402(eISSN)
Примечания : Cited References:88. - The research was supported by the Russian Science Foundation, project No. 15-19-10041.
Предметные рубрики: NADHFMN-OXIDOREDUCTASE-LUCIFERASE
HUMIC SUBSTANCES
BIOLUMINESCENT
Ключевые слова (''Своб.индексиров.''): 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.
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kratasyuk V. A., Esimbekova E. N.
Заглавие : Applications of luminous bacteria enzymes in toxicology
Место публикации : Comb. Chem. High Throughput Screen. - 2015. - Vol. 18, Is. 10. - С. 952-959. - ISSN 13862073 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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