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1.


   
    Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase / A. Bezrukikh [et al.] // . - 2014, DOI 10.1007/s00216-014-7987-1 . - ISSN 1618-2642
Кл.слова (ненормированные):
Bacterial luciferase -- Bioluminescence -- Gelatin -- NADH:FMN-oxidoreductase -- Stabilization of enzymes -- Starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 °C and 25 °C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 °C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions. © 2014 Springer-Verlag Berlin Heidelberg.

Scopus
Держатели документа:
Laboratory of Bioluminescent Biotechnologies, Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi 79, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A.; Esimbekova, E.; Nemtseva, E.; Kratasyuk, V.; Shimomura, O.

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2.


   
    Gelatin and Starch Media Stabilize Bacterial Luciferase and Oxidoreductase [Text] / A. . Bezrukikh, E. . Esimbekova, V. . Kratasyuk // Luminescence. - 2014. - Vol. 29. - P73-74. - Cited References: 2 . - ISSN 1522-7235. - ISSN 1522-7243

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

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

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3.


   
    Gelatin and starch as stabilizers of the coupled enzyme system of luminous bacteria NADH:FMN-oxidoreductase-luciferase [Text] / A. . Bezrukikh [et al.] // Anal. Bioanal. Chem. - 2014. - Vol. 406, Is. 23. - P5743-5747, DOI 10.1007/s00216-014-7987-1. - Cited References: 14. - The work was supported by the Program of the Government of Russian Federation "Measures to attract leading scientists to Russian educational institutions" (grant no. 11.G34.31.0058), the Russian Academy of Sciences (program "Molecular and Cell Biology", grant no. 6.8), and the state contract between the Ministry of Education and Science and Siberian Federal University, no. 1762. . - ISSN 1618-2642. - ISSN 1618-2650
РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
IMMOBILIZATION
   CHEMISTRY
Кл.слова (ненормированные):
Bacterial luciferase -- NADH:FMN-oxidoreductase -- Bioluminescence -- Stabilization of enzymes -- Gelatin -- Starch
Аннотация: We have studied the effects of a gel-like environment on the characteristics of enzyme preparations based on the coupled enzyme system of luminous bacteria, NADH:FMN-oxidoreductase-luciferase, to design a stable immobilizing reagent for bioluminescent analysis. Natural polymers, gelatin and starch, were used to create a viscous, structured microenvironment. The stability of the coupled enzyme system to such physical and chemical environmental factors as temperature, pH, and ionic strength in gelatin and starch-containing media was examined. It was shown that both gelatin and starch have a stabilizing effect on the enzymes of luminous bacteria under specific conditions. In particular, the enzymes' activity is increased twofold in the presence of 1 and 5 % of gelatin at 20 A degrees C and 25 A degrees C, respectively (temperatures lower than the gel point). Also, the acceptable pH range of the coupled enzyme system expands into the alkaline region and becomes 6.8-8.1. Stabilization at low ionic strength (0.01-0.06 mol L-1) is observed. At the same time, microenvironments based on either gelatin or starch do not change the enzymes' thermal inactivation rate constants in the temperature range from 25 to 43 A degrees C. Finally, gelatin and starch are suitable for development of a reagent for immobilization of enzymes which would be stable and resistant to physical and chemical environmental conditions.

WOS
Держатели документа:
[Bezrukikh, Anna
Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina
Shimomura, Osamu] Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia
[Esimbekova, Elena
Nemtseva, Elena
Kratasyuk, Valentina] Inst Biophys SB RAS, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bezrukikh, A...; Esimbekova, E...; Nemtseva, E...; Kratasyuk, V...; Shimomura, O...; Government of Russian Federation [11.G34.31.0058]; Russian Academy of Sciences [6.8]; Ministry of Education and Science [1762]; Siberian Federal University [1762]

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4.


   
    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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5.


   
    Impact of enzyme stabilizers on the characteristics of biomodules for bioluminescent biosensors / V. Lonshakova-Mukina, E. Esimbekova, V. Kratasyuk // Sens Actuators, B Chem. - 2015. - Vol. 213. - P244-247, DOI 10.1016/j.snb.2015.02.061 . - ISSN 0925-4005
Кл.слова (ненормированные):
Bioluminescence -- Body fluids -- Carrier concentration -- Enzymes -- Starch -- Bioluminescent biosensor -- Bovine serum albumins -- Dithiothreitol -- Maximum permissible concentration -- Mercaptoethanol -- Oxidoreductases -- Storage stability -- Toxic substances -- Biosensors
Аннотация: The biomodule of bioluminescent biosensor based on a coupled enzyme system NADH:FMN-oxidoreductase and luciferase, co-immobilized with substrates in dried starch or gelatin gels, has been developed. We studied the impact of several stabilizers - dithiothreitol (DTT), bovine serum albumin (BSA) and mercaptoethanol (ME) on the biomodule's activity, storage stability and sensitivity to toxic substances. The inclusion of stabilizers increases the activity of the biological module by more than 150%. To achieve the combination of high activity, prolonged storage time and acute sensitivity to toxic substances within maximum permissible concentration we used starch gel as a carrier adding 100 ?M DTT to the immobilized preparation. The gelatin-based biological module had greater storage stability than the starch-based one but demonstrated less sensitivity to toxic substances. © 2015 Elsevier B.V. All rights reserved.

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Держатели документа:
Institute of Fundamental Biology and Biotechnology, Siberian Federal University, pr. Svobodnyi 79Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, Akademgorodok 50/50Krasnoyarsk, Russian Federation
ИБФ СО РАН

Доп.точки доступа:
Lonshakova-Mukina, V.; Esimbekova, E.; Kratasyuk, V.

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6.


   
    Contrasting relationship between macro- and microviscosity of the gelatin- and starch-based suspensions and gels [Text] / D. V. Gulnov, E. V. Nemtseva, V. A. Kratasyuk // Polym. Bull. - 2016. - Vol. 73, Is. 12. - P3421-3435, DOI 10.1007/s00289-016-1664-9. - Cited References:42. - Authors thank Alexander Kheruvimov (REC "Composite Materials and Structures", SUSU, Chelyabinsk, Russia) for assistance in rheological experiments. The research was partially supported by the grants No. 11.G34.31.0058 and 1762 from The Ministry of Education and Science of the Russian Federation and by the state budget allocated to the fundamental research at the Russian Academy of Sciences (Project No. 01201351504). . - ISSN 0170-0839. - ISSN 1436-2449
РУБ Polymer Science
Рубрики:
FLUORESCENT MOLECULAR ROTORS
   INTRACELLULAR VISCOSITY
   DRUG-DELIVERY
Кл.слова (ненормированные):
Biopolymer -- Gelatin -- Starch -- Physical gel -- Microviscosity -- Molecular -- rotor
Аннотация: The problem of correlation between rheological properties in macro- and micro- scales of media with biopolymers of polypeptide (gelatin) and polysaccharide (starch) nature is investigated. The viscosity of the biopolymer solutions with concentrations 0.5-5 wt% was estimated by standard rotational rheometry technique and with fluorescent molecular rotor at 15-50 A degrees C. Opposite trends were observed for relationship between microviscosity eta (m) and macroviscosity eta for two biopolymers: eta (m) << eta for gelatin and eta (m) >> eta for starch solutions. The temperature dependence of eta (m) followed the monoexponential decay law in all samples over the whole temperature range indicating insensitivity of microviscosity to gel mesh melting under heating. The dissimilarity of macro- and micro-rheological properties of gelatin and starch-containing media is discussed in terms of difference in architecture of the gels.

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Держатели документа:
Siberian Fed Univ, Lab Bioluminescent Biotechnol, Krasnoyarsk 660041, Russia.
Inst Biophys SB RAS, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Gulnov, Dmitry V.; Nemtseva, Elena V.; Kratasyuk, Valentina A.; Ministry of Education and Science of the Russian Federation [11.G34.31.0058, 1762]; Russian Academy of Sciences [01201351504]

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7.


   
    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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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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8.


   
    Stabilization of Butyrylcholinesterase by the Entrapment into the Natural Polymer-Based Gels / V. I. Lonshakova-Mukina, E. N. Esimbekova, V. A. Kratasyuk // Doklad. Biochem. Biophys. - 2018. - Vol. 479, Is. 1. - P98-100, DOI 10.1134/S1607672918020126 . - ISSN 1607-6729
Аннотация: A new method for obtaining stable butyrylcholinesterase (BuChE) samples based on the enzyme immobilization in starch and gelatin gels followed by drying is proposed. Coimmobilization of BuChE with the thiol group indicator 5,5'-dithiobis(2-nitrobenzoic) acid did not reduce the activity of BuChE, which allowed us to simplify the procedure and reduce the time of analysis of organophosphorus pesticides. The resulting immobilized samples retained activity for at least 300 days. BuChE samples based on the starch gel showed a greater sensitivity in the determination of pesticides as compared to the samples based on the gelatin gel. © 2018, Pleiades Publishing, Ltd.

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

Доп.точки доступа:
Lonshakova-Mukina, V. I.; Esimbekova, E. N.; Kratasyuk, V. A.

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9.


   
    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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10.


   
    NAD(P)H:FMN-Oxidoreductase Functioning Under Macromolecular Crowding: In Vitro Modeling / A. E. Govorun, E. N. Esimbekova, V. A. Kratasyuk // Doklad. Biochem. Biophys. - 2019. - Vol. 486, Is. 1. - P213-215, DOI 10.1134/S160767291903013X . - ISSN 1607-6729
Аннотация: The functioning of NAD(P)H:FMN‑oxidoreductase (Red) from Vibrio fischeri under conditions of macromolecular crowding (MMC) simulated in vitro by adding biopolymers (starch and gelatin) was studied. The dissociation rate constants and the activation energies of dissociation of Red to the subunits were calculated, and the process of denaturation of Red was analyzed. It is shown that the functioning of Red both under conditions of MMC and in diluted solutions is the same. This result refutes the common belief that the native conformation of enzymes in vivo is stabilized due to MMC as compared to the in vitro conditions. © 2019, Pleiades Publishing, Ltd.

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Держатели документа:
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation

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

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11.


   
    Gelatin and Starch: What Better Stabilizes the Enzyme Activity? / E. N. Esimbekova, A. E. Govorun, V. I. Lonshakova-Mukina, V. A. Kratasyuk // Dokl. Biol. Sci. - 2020. - Vol. 491, Is. 1. - P43-46, DOI 10.1134/S0012496620020039 . - ISSN 0012-4966
Кл.слова (ненормированные):
butyrylcholinesterase -- enzyme stabilization -- gelatin -- luciferase -- NAD(P)H:FMN oxidoreductase -- starch -- thermal inactivation of enzymes
Аннотация: Abstract: The regularities of the functioning of a number of enzymes in a viscous environment created by natural polymers, starch and gelatin are examined. Based on the analysis of kinetic curves of thermal inactivation, mechanisms of thermal inactivation of enzymes in a viscous microenvironment are proposed. Using the example of butyrylcholinesterase, NAD(P)H:FMN oxidoreductase, and coupled system of the luminous bacteria (NAD(P)H:FMN oxidoreductase + luciferase), the conditions, under which starch and gelatin have a stabilizing effect on enzyme activity during storage and exposure to various physical and chemical environmental factors, were found. A significant increase in the stabilizing effect is achieved by eliminating water during drying the enzyme preparations immobilized in starch and gelatin polymer gels. © 2020, Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation

Доп.точки доступа:
Esimbekova, E. N.; Govorun, A. E.; Lonshakova-Mukina, V. I.; Kratasyuk, V. A.

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12.


   
    Thermal Inactivation of Butyrylcholinesterase in Starch and Gelatin Gels / V. I. Lonshakova-Mukina, E. N. Esimbekova, V. A. Kratasyuk // Catalysts. - 2021. - Vol. 11, Is. 4. - Ст. 492, DOI 10.3390/catal11040492. - Cited References:39. - The research was funded by the Government of Krasnoyarsk Territory, Krasnoyarsk Regional Fund of Science, and the Russian Foundation for Basic Research [project No 20-44-242001]. . - ISSN 2073-4344
РУБ Chemistry, Physical

Кл.слова (ненормированные):
butyrylcholinesterase -- thermal inactivation -- enzyme stability -- kinetics -- starch -- gelatin
Аннотация: The present study demonstrates a simple approach to enhancing thermal stability of butyrylcholinesterase (BChE) by using natural polymers. Analysis of thermal inactivation of the tetrameric BChE in starch and gelatin gels at 50-64 degrees C showed that thermal inactivation followed second-order kinetics and involved two alternating processes of BChE inactivation, which occurred at different rates (fast and slow processes). The activation enthalpy Delta H-# and the activation entropy Delta S-# for BChE in starch and gelatin gels were evaluated. The values of Delta H-# for the fast and the slow thermal inactivation of BChE in starch gel were 61 +/- 3, and 22 +/- 2 kcal/mol, respectively, and the values of Delta S-# were 136 +/- 12 and -2.03 +/- 0.05 cal center dot K-1 center dot mol(-1), respectively. Likewise, the values of Delta H-# for BChE in gelatin gel were 58 +/- 6 and 109 +/- 11 kcal/mol, and the values of Delta S-# were 149 +/- 16 and 262 +/- 21 cal center dot K-1 center dot mol(-1), respectively. The values of the activation parameters obtained in this study suggest that starch gel produced a stronger stabilizing effect on BChE exposed to elevated temperatures over long periods compared with gelatin gel.

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Держатели документа:
Siberian Fed Univ, Inst Fundamental Biol & Biotechnol, Biophys Dept, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Lonshakova-Mukina, Victoria I.; Esimbekova, Elena N.; Kratasyuk, Valentina A.; Government of Krasnoyarsk Territory; Krasnoyarsk Regional Fund of Science; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [20-44-242001]

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