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Кратасюк, В. А.
Использование светящихся бактерий в биолюминесцентном анализе [Текст] : научное издание / В. А. Кратасюк, И. И. Гительзон // Успехи микробиол. - 1987. - N 21. - С. 3-30 . - ISSN 0566-392X

ГРНТИ

34.15.33

РУБ 343.15.33
Рубрики:
БАКТЕРИИ
   СВЕТЯЩИЕСЯ КУЛЬТУРЫ
   СВОЙСТВА
   ИММОБИЛИЗОВАННЫЙ ФЕРМЕНТ
   ПОЛУЧЕНИЕ
   ПРИМЕНЕНИЕ
   БИОЛЮМИНЕСЦЕНТНЫЙ АНАЛИЗ
   ОБЩИЕ ПРИНЦИПЫ
   ОБЗОРЫ
   БИБЛ 161
   IMMOBILIZED ENZYMES
   В О М Е СЕ СЕ

Доп.точки доступа:
Гительзон, И.И.

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Creation of Bifunctional Indicating Complex Based on Nanodiamonds and Extracellular Oxidases of Luminous Fungus Neonothopanus nambi / O. A. Mogilnaya [et al.] // Dokl. Biochem. Biophys. - 2018. - Vol. 480, Is. 1. - P135-138, DOI 10.1134/S160767291803002X. - Cited References:13 . - ISSN 1607-6729. - ISSN 1608-3091

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PHANEROCHAETE-CHRYSOSPORIUM
NANOPARTICLES
Аннотация: A bifunctional indicating complex was created by immobilization of extracellular oxidases (glucose oxidase and peroxidases) of luminous fungus Neonothopanus nambi onto modified nanodiamonds (MNDs) synthesized by detonation. It was found that the enzymes firmly adsorb onto MND particles and exhibit their catalytic activity. Model in vitro experiments showed that the created MND-enzymes complex is suitable for repeated use for analyte (glucose and phenol) testing and retains its activity after storage at 4 degrees C in deionized water for 1 month. The data obtained offer the prospects for developing a new class of reusable multifunctional indicating and diagnostic test systems on the basis of MNDs and higher fungal enzymes for medical and ecological analytics.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk, Russia.

Доп.точки доступа:
Mogilnaya, O. A.; Ronzhin, N. O.; Artemenko, K. S.; Bondar, V. S.

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Bioluminescent and structural features of native folded Gaussia luciferase / M. D. Larionova, S. V. Markova, E. S. Vysotski // J. Photochem. Photobiol. B Biol. - 2018. - Vol. 183. - P309-317, DOI 10.1016/j.jphotobiol.2018.04.050 . - ISSN 1011-1344
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Copepod luciferase -- Halophilic enzyme -- Kinetic cooperativity
Аннотация: The secreted luciferases responsible for light emission of marine copepods have gained popularity for being used in noninvasive imaging of intracellular events. The secreted luciferase of copepod Gaussia princeps is a one-subunit protein catalyzing coelenterazine oxidation to emit blue light. It consists of the N-terminal variable part that bears a signal peptide for secretion and the C-terminal catalytic domain containing ten highly conserved Cys residues supposing the existence of up to five S–S bonds. Despite wide application of Gaussia luciferase in biomedical research, its biochemical properties are still insufficiently studied due to the general problem of obtaining the proper folded Cys-rich proteins in bacterial cells. Here we report the properties of the proper folded Gaussia luciferase produced in insect cells using baculovirus expression system. This high purity luciferase reveals the highest activity at 15–20 °C but retains only ~20% activity at 37 °C that may hamper its application for in vivo assays. The maximum of bioluminescent activity of GpLuc is found at NaCl concentrations in the range of 1.0–1.5 M and, furthermore, a high NaCl concentration enhances luciferase stability to thermal denaturation, i.e. Gaussia luciferase displays the features characteristic of halophilic enzymes. The studies on bioluminescence kinetics at different coelenterazine concentrations obviously show a positive cooperativity of Gaussia luciferase with coelenterazine (Hill coefficient – 1.8 ± 0.2; K0.5–2.14 ± 0.17 ?M). We suggest this effect to be rather due to the so-called kinetic cooperativity conditioned by conformational changes in response to substrate binding than to the presence of two catalytic sites. © 2018 Elsevier B.V.

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Держатели документа:
Photobiology Laboratory, Institute of Biophysics SB RAS, Federal Research Center “Krasnoyarsk Science Center SB RAS”, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Larionova, M. D.; Markova, S. V.; Vysotski, E. S.

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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.

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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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Estimating levels of light emission and extracellular peroxidase activity of mycelium of luminous fungus Neonothopanus nambi treated with ?-glucosidase / O. A. Mogilnaya, N. O. Ronzhin, V. S. Bondar // Curr. Res. Environ. Appl. Mycol. J. Fungal. - 2018. - Vol. 8, Is. 1. - P75-85, DOI 10.5943/cream/8/1/6 . - ISSN 2229-2225
Кл.слова (ненормированные):
Basidiomycetes -- Cell wall -- Luminescence -- Polysaccharide sheath
Аннотация: The present study estimates the level of extracellular peroxidase activity and light emission intensity of mycelium of luminescent basidiomycete Neonothopanus nambi treated with ?-glucosidase. A hypothesis has been proposed that treatment with ?-glucosidase may trigger biochemical mechanisms of activation of ROS (primarily hydrogen peroxide) generation in N. nambi mycelium. The results obtained indicate that the enzyme causes partial disintegration of the slimy sheath of fungal hyphae and intracellular matrix, which leads to release of the extracellular peroxidases to the incubation medium. Mycelial cells treated with the enzyme reach the peak of their luminescence sooner. It has been assumed that partial loss of extracellular peroxidases, as important enzymes of antioxidant defense, may be compensated for by an increase in the level of light emission by the fungus. © 2018 Beijing Academy of Agriculture and Forestry Sciences.

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Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center Krasnoyarsk Science Center SB RAS, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Mogilnaya, O. A.; Ronzhin, N. O.; Bondar, V. S.

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Genetically encodable bioluminescent system from fungi / A. A. Kotlobay [et al.] // Proc. Natl. Acad. Sci. U. S. A. - 2018. - Vol. 115, Is. 50. - P12728-12732, DOI 10.1073/pnas.1803615115 . - ISSN 0027-8424
Кл.слова (ненормированные):
Bioluminescence -- Fungal luciferase -- Fungal luciferin biosynthesis
Аннотация: Bioluminescence is found across the entire tree of life, conferring a spectacular set of visually oriented functions from attracting mates to scaring off predators. Half a dozen different luciferins, molecules that emit light when enzymatically oxidized, are known. However, just one biochemical pathway for luciferin biosynthesis has been described in full, which is found only in bacteria. Here, we report identification of the fungal luciferase and three other key enzymes that together form the biosynthetic cycle of the fungal luciferin from caffeic acid, a simple and widespread metabolite. Introduction of the identified genes into the genome of the yeast Pichia pastoris along with caffeic acid biosynthesis genes resulted in a strain that is autoluminescent in standard media. We analyzed evolution of the enzymes of the luciferin biosynthesis cycle and found that fungal bioluminescence emerged through a series of events that included two independent gene duplications. The retention of the duplicated enzymes of the luciferin pathway in nonluminescent fungi shows that the gene duplication was followed by functional sequence divergence of enzymes of at least one gene in the biosynthetic pathway and suggests that the evolution of fungal bioluminescence proceeded through several closely related stepping stone nonluminescent biochemical reactions with adaptive roles. The availability of a complete eukaryotic luciferin biosynthesis pathway provides several applications in biomedicine and bioengineering. © 2018 National Academy of Sciences. All Rights Reserved.

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Держатели документа:
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russian Federation
Planta LLC, Moscow, 121205, Russian Federation
Institute of Science and Technology Austria, Klosterneuburg, 3400, Austria
Medical Research Council London Institute of Medical Sciences, Imperial College London, London, W12 0NN, United Kingdom
Centre for Genomic Regulation, Barcelona Institute for Science and Technology, Barcelona, 08003, Spain
Universitat Pompeu Fabra, Barcelona, 08003, Spain
Evrogen JSC, Moscow, 117997, Russian Federation
Institute of Biophysics, Federal Research Center Krasnoyarsk Science Center, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Moscow, 142290, Russian Federation
Pirogov Russian National Research Medical University, Moscow, 117997, Russian Federation
Biomedical Nanomaterials, National Research Technological University (MISiS), Moscow, 119049, Russian Federation
Skolkovo Institute of Science and Technology, Moscow, 121205, Russian Federation
Departamento de Bioquimica, Instituto de Quimica, Universidade de Sao Paulo, Sao Paulo, 05508-000, Brazil
Departamento de Oceanografia Fisica, Quimica e Geologica, Instituto Oceanografico, Universidade de Sao Paulo, Sao Paulo, 05508-120, Brazil
Department of Environmental Biology, Chubu University, Kasugai, 487-8501, Japan
Catalan Institution for Research and Advanced Studies (ICREA), Barcelona, 08010, Spain
Departamento de Quimica Fundamental, Instituto de Quimica, Universidade de Sao Paulo, Sao Paulo, 05508-000, Brazil

Доп.точки доступа:
Kotlobay, A. A.; Sarkisyan, K. S.; Mokrushina, Y. A.; Marcet-Houben, M.; Serebrovskaya, E. O.; Markina, N. M.; Somermeyer, L. G.; Gorokhovatsky, A. Y.; Vvedensky, A.; Purtov, K. V.; Petushkov, V. N.; Rodionova, N. S.; Chepurnyh, T. V.; Fakhranurova, L. I.; Guglya, E. B.; Ziganshin, R.; Tsarkova, A. S.; Kaskova, Z. M.; Shender, V.; Abakumov, M.; Abakumova, T. O.; Povolotskaya, I. S.; Eroshkin, F. M.; Zaraisky, A. G.; Mishin, A. S.; Dolgov, S. V.; Mitiouchkina, T. Y.; Kopantzev, E. P.; Waldenmaier, H. E.; Oliveira, A. G.; Oba, Y.; Barsova, E.; Bogdanova, E. A.; Gabaldon, T.; Stevani, C. V.; Lukyanov, S.; Smirnov, I. V.; Gitelson, J. I.; Kondrashov, F. A.; Yampolsky, I. V.

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Nanodiamonds as an effective adsorbent for immobilization of extracellular peroxidases from luminous fungus Neonothopanus nambi to construct a phenol detection system / O. Mogilnaya [et al.] // Biocatal. Biotransform. - 2019. - Vol. 37, Is. 2. - P97-105, DOI 10.1080/10242422.2018.1472586. - Cited References:50. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences [project no. 0356-2016-0709]. . - ISSN 1024-2422. - ISSN 1029-2446

РУБ Biochemistry & Molecular Biology + Biotechnology & Applied Microbiology
Рубрики:
CARBON NANOTUBES
   ARMILLARIA-BOREALIS
   LIGHT-EMISSION
   DEGRADATION
Кл.слова (ненормированные):
Nanodiamonds -- immobilization -- luminous fungus -- beta-glucosidase -- peroxidase -- indicator system
Аннотация: Modified nanodiamonds (MNDs) produced by detonation synthesis can be used as an effective adsorbent to immobilize extracellular peroxidases of the luminous basidiomycete Neonothopanus nambi. The enzymes are firmly immobilized on MND particles and exhibit catalytic activity. The indicator system (the MND-enzyme complex) reused many times retains its ability to catalyze reaction of co-oxidation of phenol and 4-aminoantipirine in the presence of hydrogen peroxide and remains functionally active during long-term storage (for 1 month or longer) in aqueous suspensions at 4 degrees C. MNDs and enzymes of higher fungi can be effectively used to construct new reusable indicator systems for analytical applications such as monitoring contamination of aquatic environments by phenolic compounds.

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Держатели документа:
RAS, Inst Biophys, Fed Res Ctr, Krasnoyarsk Sci Ctr,SB, Krasnoyarsk, Russia.

Доп.точки доступа:
Mogilnaya, Olga; Ronzhin, Nikita; Artemenko, Karina; Bondar, Vladimir; Russian Academy of Sciences [0356-2016-0709]

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Effect of viscosity on efficiency of enzyme catalysis of bacterial luciferase coupled with lactate dehydrogenase and NAD(P)H:FMN-Oxidoreductase / O. S. Sutormin [et al.] // Mol. Cat. - 2018. - Vol. 458. - P60-66, DOI 10.1016/j.mcat.2018.08.012 . - ISSN 2468-8231
Кл.слова (ненормированные):
Bioluminescence -- Coupling of enzymes -- In vivo simulated media -- Metabolic chain -- Protein stability
Аннотация: One of the current trends of the modern biology figures out cellular enzyme behaviour. Numerous researches look more closely at the chemical composition of creating in vivo simulated media conditions. The aim of this work was to find out a thermodynamic cooperativity of enzymes in a triple-enzyme chain (lactate dehydrogenase + NAD(P)H: FMN-oxidoreductase + bacterial luciferase) under in vivo simulated condition. The thermodynamic cooperativity effects were found out based on the influence of the viscogens (glycerol and sucrose) on the thermal stability of the triple-enzyme system. The results showed that the viscogens do not lead to an increase in the thermal stability of the triple-enzyme system. In addition, organic solvents (sucrose and glycerol) added as viscous agents to the reaction medium altered the kinetics of this triple-enzyme chain, including changing the light emission decay constant (kdec) and quantum yield of luminescence (Q). Plus, sucrose was found to be more efficient in limiting the flexibility of enzymes than glycerol. The high sensitivity of the triple-enzyme system to the viscogens may be connected with a fact that lactate dehydrogenase does not bound with couple enzyme system NAD(P)H: FMN-oxidoreductase + bacterial luciferase inside the real cell. Since this approach may be used as a method to understand the real connection between enzymes in cellular multi-enzyme metabolic chains inside the luminous bacteria cell. © 2018 Elsevier B.V.

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Держатели документа:
Department of Biophysics, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Russian Academy of Sciences, Siberian Branch, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Sutormin, O. S.; Sukovataya, I. E.; Pande, S.; Kratasyuk, V. A.

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Protein-based fluorescent bioassay for low-dose gamma radiation exposures / A. S. Petrova [et al.] // Anal. Bioanal. Chem. - 2018, DOI 10.1007/s00216-018-1282-5 . - ISSN 1618-2642
Кл.слова (ненормированные):
Bioassay -- Enzymes -- Fluorescence/luminescence -- Fluorescent protein -- Gamma radiation -- Radiotoxicity -- Efficiency -- Enzymes -- Fluorescence -- Gamma rays -- Proteins -- Proton transfer -- Fluorescence characteristics -- Fluorescence intensities -- Fluorescence spectra -- Fluorescence/luminescence -- Fluorescent protein -- Photochemical process -- Physiological liquids -- Radiotoxicity -- Bioassay
Аннотация: The study suggests an application of a coelenteramide-containing fluorescent protein (CLM-CFP) as a simplest bioassay for gamma radiation exposures. “Discharged obelin,” a product of the bioluminescence reaction of the marine coelenterate Obelia longissima, was used as a representative of the CLM-CFP group. The bioassay is based on a simple enzymatic reaction—photochemical proton transfer in the coelenteramide-apoprotein complex. Components of this reaction differ in fluorescence color, providing, by this, an evaluation of the proton transfer efficiency in the photochemical process. This efficiency depends on the microenvironment of the coelenteramide within the protein complex, and, hence, can evaluate a destructive ability of gamma radiation. The CLM-CFP samples were exposed to gamma radiation (137Cs, 2 mGy/h) for 7 and 16 days at 20 °C and 5 °C, respectively. As a result, two fluorescence characteristics (overall fluorescence intensity and contributions of color components to the fluorescence spectra) were identified as bioassay parameters. Both parameters demonstrated high sensitivity of the CLM-CFP-based bioassay to the low-dose gamma radiation exposure (up to 100 mGy). Higher temperature (20 °C) enhanced the response of CLM-CFP to gamma radiation. This new bioassay can provide fluorescent multicolor assessment of protein destruction in cells and physiological liquids under exposure to low doses of gamma radiation. [Figure not available: see fulltext.]. © 2018, Springer-Verlag GmbH Germany, part of Springer Nature.

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Держатели документа:
Krasnoyarsk State Agrarian University, Mira Avenue 90, Krasnoyarsk, Russian Federation
Siberian Federal University, Svobodnyy Ave 79, Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, FRC KSC SB RAS, Krasnoyarsk, Russian Federation
Department of Radiology, University of Pennsylvania, 3401 N Broad St., Philadelphia, PA, United States

Доп.точки доступа:
Petrova, A. S.; Lukonina, A. A.; Dementyev, D. V.; Bolsunovsky, A. Ya. ; Popov, A. V.; Kudryasheva, N. S.

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10.

Disposable luciferase-based microfluidic chip for rapid assay of water pollution / I. Denisov [et al.] // Lumin. - 2018. - Vol. 33, Is. 6. - P1054-1061, DOI 10.1002/bio.3508 . - ISSN 1522-7235
Кл.слова (ненормированные):
bioassay -- lab-on-a-chip -- luciferase -- microfluidics -- solvent bonding
Аннотация: In the present study, we demonstrate the use of a disposable luciferase-based microfluidic bioassay chip for environmental monitoring and methods for fabrication. The designed microfluidic system includes a chamber with immobilized enzymes of bioluminescent bacteria Photobacterium leiognathi and Vibrio fischeri and their substrates, which dissolve after the introduction of the water sample and thus activate bioluminescent reactions. Limits of detection for copper (II) sulfate, 1,3-dihydroxybenzene and 1,4-benzoquinone for the proposed microfluidic biosensor measured 3 ?M, 15 mM, and 2 ?M respectively, and these values are higher or close to the level of conventional environmental biosensors based on lyophilized bacteria. Approaches for entrapment of enzymes on poly(methyl methacrylate) (PMMA) plates using a gelatin scaffold and solvent bonding of PMMA chip plates under room temperature were suggested. The proposed microfluidic system may be used with some available luminometers and future portable luminescence readers. © 2018 John Wiley & Sons, Ltd.

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Держатели документа:
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS Federal Research Center'Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Denisov, I.; Lukyanenko, K.; Yakimov, A.; Kukhtevich, I.; Esimbekova, E.; Belobrov, P.

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11.

Biochemical changes causes lack of bioluminescence in fruiting bodies of Armillaria / A. P. Puzyr, S. E. Medvedeva, V. S. Bondar // Mycosphere. - 2017. - Vol. 8, Is. 1. - P9-17, DOI 10.5943/mycosphere/8/1/2 . - ISSN 2077-7000
Кл.слова (ненормированные):
Enzymes and substrate of luminescent reaction -- Kinetics of luminescence -- Luminous mycelia -- Nonluminous fruiting bodies of fungus
Аннотация: Mycelium of Armillaria species exhibit bioluminescence in nature and when cultivated on artificial nutrient media. However, fruiting bodies do not emit visible light. The present study investigates biochemical changes which cause this phenomenon. Light emission was studied in experiments with mixtures of cold and hot extracts of the luminous mycelium of Armillaria borealis IBSO 2328 and nonluminous fruiting bodies of this fungus and an unidentified species of the genus (Armillaria sp.). Hot extracts of fruiting bodies of the nonluminous Pholiota squarrosa were used as the substrate analog of the luminescent reaction, as previously this fungus had been found to contain a high amount of this substance. Control experiments showed that cold extracts of A. borealis IBSO 2328 mycelium contained enzymes for the luminescent reaction, which is initiated after addition hot extracts of P. squarrosa fruiting bodies. Parallel experiments with extracts of the fruiting bodies of Armillaria showed that: (i) - cold extracts did not contain enzymes of the luminescent reaction or contain very small amounts of these enzymes and (ii) - hot extracts did not contain substrate of the luminescent reaction. Thus, the reason why fruiting bodies of Armillaria do not emit light is that they do not contain components required for visible luminescence. The study discusses possible causes why the enzymes and substrate of the luminescent reaction are not synthesized in fruiting bodies of Armillaria. © Guizhou Academy of Agricultural Sciences.

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Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Bondar, V. S.

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12.

Inhibition effect of food preservatives on endoproteinases / E. N. Esimbekova [et al.] // Food Chem. - 2017. - Vol. 235. - P294-297, DOI 10.1016/j.foodchem.2017.05.059 . - ISSN 0308-8146
Кл.слова (ненормированные):
Endoproteinases -- Food additives -- Pancreatic disease -- Pancreatic enzymes -- Benzoic acid -- Enzyme activity -- Enzymes -- Food additives -- Food preservatives -- Potassium sorbate -- Sodium -- Acceptable daily intakes -- Decay constants -- Endoproteinases -- Human metabolisms -- Inhibition effect -- Light intensity -- Protein digestion -- Sodium benzoate -- Sorbic acid
Аннотация: The present manuscript proposes a novel approach to assess the impact of food additives on human metabolism by analysing their effect on biomarker enzyme activity. Alterations in the activity of pancreatic enzymes, such as chymotrypsin and trypsin, which are affected by the most common food preservatives, sodium benzoate (E211), potassium sorbate (E202) and sorbic acid (E200), have been evaluated. The proteinase activity was analysed with a bioluminescent method using the light intensity decay constant. Our study revealed that the preservatives reduce proteinase activity by 50% (EC50) at a much lower concentration than their acceptable daily intake (ADI). Thus, sodium benzoate and sorbic acid have an inhibition effect on chymotrypsin at concentrations 14 times lower and 70 times lower than their ADI and this increases with exposure time. Food preservative consumption impacts negatively on protein digestion, which is especially dangerous for patients with pancreatitis. © 2017 Elsevier Ltd

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Держатели документа:
Institute of Biophysics SB RAS, Federal Research Center ‘Krasnoyarsk Science Center SB RAS’, Krasnoyarsk, Russian Federation
Siberian Federal University, Institute of Fundamental Biology and Biotechnology, Krasnoyarsk, Russian Federation
Krasnoyarsk State Agricultural University, Institute of Agro-ecological Technologies, Krasnoyarsk, Russian Federation

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

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13.

Rapid biosensing tools for cancer biomarkers / R. Ranjan, E. N. Esimbekova, V. A. Kratasyuk // Biosens. Bioelectron. - 2017. - Vol. 87. - P918-930, DOI 10.1016/j.bios.2016.09.061. - Cited References:115. - The research was partially supported by the Russian Foundation for Basic Research (Project no. 16-34-60100 and No. 16-06-00439), the state budget allocated to the fundamental research Russian Academy of Sciences (Project no. 01201351504). . - ISSN 0956-5663. - ISSN 1873-4235

РУБ Biophysics + Biotechnology & Applied Microbiology + Chemistry, Analytical
Рубрики:
POINT-OF-CARE
   HIGHLY SENSITIVE DETECTION
   ACOUSTIC-WAVE BIOSENSOR
   DNA
Кл.слова (ненормированные):
Biosensor -- Cancer biomarker -- Functional nanomaterials -- Point-of-care -- devices -- Microfluidics
Аннотация: The present review critically discusses the latest developments in the field of smart diagnostic systems for cancer biomarkers. A wide coverage of recent biosensing approaches involving aptamers, enzymes, DNA probes, fluorescent probes, interacting proteins and antibodies in vicinity to transducers such as electrochemical, optical and piezoelectric is presented. Recent advanced developments in biosensing approaches for cancer biomarker owes much credit to functionalized nanomaterials due to their unique opto-electronic properties and enhanced surface to volume ratio. Biosensing methods for a plenty of cancer biomarkers has been summarized emphasizing the key principles involved.

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Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Dept Biophys, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Akademgorodok 50-50, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Ranjan, Rajeev; Esimbekova, Elena N.; Kratasyuk, Valentina A.; Russian Foundation for Basic Research [16-34-60100, 16-06-00439]; state budget allocated to the fundamental research Russian Academy of Sciences Project [01201351504]

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14.

On mechanism of antioxidant effect of fullerenols / A. S. Sachkova [et al.] // Biochem. Biophys. Rep. - 2017. - Vol. 9. - P1-8, DOI 10.1016/j.bbrep.2016.10.011 . - ISSN 2405-5808
Кл.слова (ненормированные):
Antioxidant activity -- Bacterial enzymes -- Fullerenol -- Hormesis -- Luminous marine bacteria -- Ultralow concentrations
Аннотация: Fullerenols are nanosized water-soluble polyhydroxylated derivatives of fullerenes, specific allotropic form of carbon, bioactive compounds and perspective pharmaceutical agents. Antioxidant activity of fullerenols was studied in model solutions of organic and inorganic toxicants of oxidative type – 1,4-benzoquinone and potassium ferricyanide. Two fullerenol preparations were tested: С60О2–4(ОН)20–24 and mixture of two types of fullerenols С60О2–4(ОН)20–24+С70О2–4(ОН)20–24. Bacteria-based and enzyme-based bioluminescent assays were used to evaluate a decrease in cellular and biochemical toxicities, respectively. Additionally, the enzyme-based assay was used for the direct monitoring of efficiency of the oxidative enzymatic processes. The bacteria-based and enzyme-based assays showed similar peculiarities of the detoxification processes: (1) ultralow concentrations of fullerenols were active (ca 10–17–10?4 and 10–17–10? 5 g/L, respectively), (2) no monotonic dependence of detoxification efficiency on fullerenol concentrations was observed, and (3) detoxification of organic oxidizer solutions was more effective than that of the inorganic oxidizer. The antioxidant effect of highly diluted fullerenol solutions on bacterial cells was attributed to hormesis phenomenon; the detoxification was concerned with stimulation of adaptive cellular response under low-dose exposures. Sequence analysis of 16S ribosomal RNA was carried out; it did not reveal mutations in bacterial DNA. The suggestion was made that hydrophobic membrane-dependent processes are involved to the detoxifying mechanism. Catalytic activity of fullerenol (10? 8 g/L) in NADH-dependent enzymatic reactions was demonstrated and supposed to contribute to adaptive bacterial response. © 2016 The Authors

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Держатели документа:
National Research Tomsk Polytechnic University, Tomsk, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Physics SB RAS, Krasnoyarsk, Russian Federation
SB RAS Genomics Core Facility, Institute of Chemical Biology and Fundamental Medicine SB RAS, Novosibirsk, Russian Federation

Доп.точки доступа:
Sachkova, A. S.; Kovel, E. S.; Churilov, G. N.; Guseynov, O. A.; Bondar, A. A.; Dubinina, I. A.; Kudryasheva, N. S.

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15.

Salinity modulates thermotolerance, energy metabolism and stress response in amphipods Gammarus lacustris / K. P. Vereshchagina [et al.] // PeerJ. - 2016. - Vol. 2016, Is. 11, DOI 10.7717/peerj.2657 . - ISSN 2167-8359
Кл.слова (ненормированные):
Adaptation -- Amphipoda -- Gammarus lacustris -- Salinity -- Thermal tolerance
Аннотация: Temperature and salinity are important abiotic factors for aquatic invertebrates. We investigated the influence of different salinity regimes on thermotolerance, energy metabolism and cellular stress defense mechanisms in amphipods Gammarus lacustris Sars from two populations. We exposed amphipods to different thermal scenarios and determined their survival as well as activity of major antioxidant enzymes (peroxidase, catalase, glutathione S-transferase) and parameters of energy metabolism (content of glucose, glycogen, ATP, ADP, AMP and lactate). Amphipods from a freshwater population were more sensitive to the thermal challenge, showing higher mortality during acute and gradual temperature change compared to their counterparts from a saline lake. A more thermotolerant population from a saline lake had high activity of antioxidant enzymes. The energy limitations of the freshwater population (indicated by low baseline glucose levels, downward shift of the critical temperature of aerobic metabolism and inability to maintain steady-state ATP levels during warming) was ob- served, possibly reflecting a trade-off between the energy demands for osmoregulation under the hypo-osmotic condition of a freshwater environment and protection against temperature stress. © 2016 Vereshchagina et al.

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Institute of Biology, Irkutsk State University, Irkutsk, Russian Federation
Baikal Research Centre, Irkutsk, Russian Federation
Institute of Biophysics SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute for Biological Sciences, University of Rostock, Rostock, Germany

Доп.точки доступа:
Vereshchagina, K. P.; Lubyaga, Y. A.; Shatilina, Z.; Bedulina, D.; Gurkov, A.; Axenov-Gribanov, D. V.; Baduev, B.; Kondrateva, E. S.; Gubanov, M.; Zadereev, E.; Sokolova, I.; Timofeyev, M.

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16.

Morphological properties and levels of extracellular peroxidase activity and light emission of the basidiomycete Armillaria borealis treated with beta-glucosidase and chitinase / O. A. Mogilnaya [et al.] // Mycosphere. - 2017. - Vol. 8, Is. 4. - P649-+, DOI 10.5943/mycosphere/8/4/11. - Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences (project no. 0356-2016-0709) and Program No. II. 2 "Integration and Development" of the Siberian Branch of the Russian Academy of Sciences (project no. 0356-2015-0103). . - ISSN 2077-7000

РУБ Mycology
Рубрики:
FUNGAL CELL-WALL
OXIDATIVE STRESS
PHANEROCHAETE-CHRYSOSPORIUM
Кл.слова (ненормированные):
basidiomycetes -- bioluminescence -- cell wall -- beta-glucosidase -- chitinase -- peroxidase
Аннотация: The study estimates morphological properties and levels of extracellular peroxidase activity and light emission of mycelium of the basidiomycete Armillaria borealis IBSO 2328 treated with beta-glucosidase and chitinase. Mycelium incubated with the enzymes shows considerable morphological changes and indications of osmotic shock. Injuries observed in the cell envelope of the fungal hyphae are primarily attributed to the partial (in the beta-glucosidase treatment) or complete (in the chitinase treatment) disintegration of the melanin layer on the surface of the cell wall. Changes in the cell wall of hyphae are accompanied by release of extracellular peroxidases of the fungus into the incubation medium and an increase in light emission relative to the luminescence of the control pellets. We assume that higher level of luminescence of the enzyme-treated mycelium samples could be related to the disintegration of the surface pigment layer of the hyphae and the partial loss of extracellular peroxidases. The data obtained confirm the previously proposed hypothesis in which light producing reaction of the fungus may be an additional way to neutralize active oxygen radicals under stress.

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Держатели документа:
Russian Acad Sci, Siberian Branch, Inst Biophys, Fed Res Ctr Krasnoyarsk Sci Ctr SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Mogilnaya, O. A.; Ronzhin, N. O.; Artemenko, K. S.; Bondar, V. S.; Russian Academy of Sciences [0356-2016-0709, 0356-2015-0103]

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17.

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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18.

Luminescence of cold extracts from mycelium of luminous basidiomycetes during long-term storage / A. P. Puzyr [et al.] // Curr. Res. Environ. Appl. Mycol. J. Fungal. - 2017. - Vol. 7, Is. 3. - P227-235, DOI 10.5943/cream/7/3/9 . - ISSN 2229-2225
Кл.слова (ненормированные):
Armillaria borealis -- Kinetics of luminescence -- Lyophilic preparations -- Mycena citricolor -- Neonothopanus nambi
Аннотация: Cold extracts with high activities of enzymes of luminescent reaction were prepared from mycelia of luminous fungi Armillaria borealis IBSO 2328, Mycena citricolor IBSO 2331, and Neonothopanus nambi IBSO 2391. The authors describe techniques of preparing cold extracts with high levels of luminescence from mycelial biomass of different species of luminous basidiomycetes. The investigation of cold extracts showed that in experiments with freezing and thawing of the samples as well as in experiments with lyophilization followed by dissolution of the dry samples, the levels of enzyme activity were high, with in vitro luminescence exhibited after addition of NADPH and the hot extract containing the substrate. High activity levels of the enzymes of luminescent reaction were measured in lyophilized cold extracts stored over three years. In lyophilized preparations, the enzymes of luminescent reaction had high thermostability, even when dry preparations of cold extracts were exposed to a temperature of 100°C for 60 minutes. © Beijing Academy of Agriculture and Forestry Sciences.

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Institute of Biophysics, Siberian Branch of Russian Academy of Science, Federal Research Center 'Krasnoyarsk Science Center SB RAS', Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Puzyr, A. P.; Medvedeva, S. E.; Artemenko, K. S.; Bondar, V. S.

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19.

Active mixing of immobilised enzymatic system in microfluidic chip / K. A. Lukyanenko [et al.] // Micro Nano Lett. - 2017. - Vol. 12, Is. 6. - P377-381, DOI 10.1049/mnl.2016.0646. - Cited References:17. - The research was supported by the grant of the Russian Science Foundation (project no. 15-19-10041). . - ISSN 1750-0443

РУБ Nanoscience & Nanotechnology + Materials Science, Multidisciplinary
Рубрики:
POLY(METHYL METHACRYLATE)
   SURFACE MODIFICATION
   POINT
   DEVICES
   PMMA
Аннотация: Parameters for sample introduction, dried reagents dissolution and mixing with sample for bienzyme system NAD(H):FMN-oxidoreductase and luciferase immobilised in microfluidic chip were successfully determined. Numerical simulations of reaction chamber geometry, flavin mononucleotide (FMN) escape from starch gel and mixing options were conducted to achieve higher sensitivity of bioluminescent reaction. Results of numerical simulations were verified experimentally. The active mixer for dried reagents was made from an electro-mechanical speaker's membrane which was connected to the input of the chip. Such a mixer provided better efficiency than a passive mixing, and it is simple enough for use in point-of-care devices with any systems based on immobilised enzymes in chips.

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Держатели документа:
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
ITMO Univ, St Petersburg 197101, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.
Inst Analyt Instrumentat, St Petersburg 198095, Russia.

Доп.точки доступа:
Lukyanenko, Kirill A.; Belousov, Kirill I.; Denisov, Ivan A.; Yakimov, Anton S.; Esimbekova, Elena N.; Bukatin, Anton S.; Evstrapov, Anatoly A.; Belobrov, Peter I.; Russian Science Foundation [15-19-10041]

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20.

Why does the bioluminescent fungus Armillaria mellea have luminous mycelium but nonluminous fruiting body? / K. V. Purtov [et al.] // Doklad. Biochem. Biophys. - 2017. - Vol. 474, Is. 1. - P217-219, DOI 10.1134/S1607672917030176 . - ISSN 1607-6729
Аннотация: By determining the components involved in the bioluminescence process in luminous and nonluminous organs of the honey fungus Armillaria mellea, we have established causes of partial luminescence of this fungus. The complete set of enzymes and substrates required for bioluminescence is formed only in the mycelium and only under the conditions of free oxygen access. Since the synthesis of luciferin precursor (hispidin) and 3-hydroxyhispidin hydroxylase in the fruiting bodies is blocked, the formation of luciferin—the key component of fungal bioluminescent system—was not observed. That is why the fruiting body of Armillaria mellea is nonluminous despite the presence of luciferase, the enzyme that catalyzes the oxidation of luciferin with a photon emission. © 2017, Pleiades Publishing, Ltd.

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Держатели документа:
Institute of Biophysics, Krasnoyarsk Research Center, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Purtov, K. V.; Petushkov, V. N.; Rodionova, N. S.; Gitelson, J. I.

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