Библиотека института биофизики СО РАН

Главная

Базы данных

Труды сотрудников ИБФ СО РАН - результаты поиска

Вид поиска

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН

Иностранные журналы библиотеки Института биофизики СО РАН

Отечественные журналы библиотеки Института биофизики СО РАН

Каталог диссертаций ИБФ СО РАН

Труды сотрудников ИБФ СО РАН

Область поиска

Найдено в других БД:

Каталог книг и продолжающихся изданий библиотеки Института биофизики СО РАН (2)

Формат представления найденных документов:
полный	информационный	краткий

Отсортировать найденные документы по:
автору	заглавию	году издания	типу документа

Поисковый запрос: (<.>K=immobilization<.>)

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

Carbon Monoxide Absorption by Immobilized Cells of Carboxidobacteria / T. G. Volova, V. F. Plotnikov // Prikladnaya Biokhimiya i Mikrobiologiya. - 1999. - Vol. 35, Is. 1. - С. 44 . - ISSN 0555-1099
Аннотация: Immobilization in gels was shown to stabilize the CO-oxidase activity of whole cells of the carboxidobacterium Seliberia carboxydohydrogena. The half-inactivation time of the immobilized preparations was up to 50 days. The fundamental possibility of the use of immobilized cells of carboxidobacteria for removing carbon monoxide from air was demonstrated with laboratory prototype models of biological filters.

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

Доп.точки доступа:
Volova, T.G.; Plotnikov, V.F.

Найти похожие

Carbon monoxide absorption by immobilized cells of carboxidobacteria / T. G. Volova, V. F. Plotnikov // Applied Biochemistry and Microbiology. - 1999. - Vol. 35, Is. 1. - P38-39 . - ISSN 0003-6838
Аннотация: Immobilization in gels was shown to stabilize the CO-oxidase activity of whole cells of the carboxidobacterium Seliberia carboxydohydrogena. The inactivation half-time of the immobilized preparations was up to 50 days. The fundamental possibility of the use of immobilized cells of carboxidobacteria for removing carbon monoxide from air was demonstrated with laboratory prototype models of biological filters.

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

Доп.точки доступа:
Volova, T.G.; Plotnikov, V.F.

Найти похожие

Nanodiamonds as Carriers for Address Delivery of Biologically Active Substances [Text] / K. V. Purtov [et al.] // Nanoscale Res. Lett. - 2010. - Vol. 5, Is. 3. - P631-636, DOI 10.1007/s11671-010-9526-0. - Cited References: 24. - This work was supported by the Program # 27 for Basic Research of the Presidium of RAS (project 3.6.3). . - ISSN 1931-7573

РУБ Nanoscience & Nanotechnology + Materials Science, Multidisciplinary + Physics, Applied
Рубрики:
ANTICANCER DRUGS
   NANOPARTICLES
   ADSORPTION
   PARTICLES
   PROTEINS
Кл.слова (ненормированные):
Nanodiamonds -- Ligand -- Protein immobilization -- Nanocarrier -- Targeted delivery
Аннотация: Surface of detonation nanodiamonds was functionalized for the covalent attachment of immunoglobulin, and simultaneously bovine serum albumin and Rabbit Anti-Mouse Antibody. The nanodiamond-IgG(I125) and RAM-nanodiamond-BSA(I125) complexes are stable in blood serum and the immobilized proteins retain their biological activity. It was shown that the RAM-nanodiamond-BSA(I125) complex is able to bind to the target antigen immobilized on the Sepharose 6B matrix through antibody-antigen interaction. The idea can be extended to use nanodiamonds as carriers for delivery of bioactive substances (i.e., drugs) to various targets in vivo.

Держатели документа:
[Purtov, K. V.
Puzyr, A. P.
Bondar, V. S.] SB RAS, Inst Biophys, Krasnoyarsk, Russia
[Petunin, A. I.] Med Res Co Dias, Krasnoyarsk, Russia
[Burov, A. E.] SB RAS, Inst Computat Modeling, Krasnoyarsk, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Purtov, K.V.; Petunin, A.I.; Burov, A.E.; Puzyr, A.P.; Bondar, V.S.

Найти похожие

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.

Найти похожие

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]

Найти похожие

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

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

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

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

Найти похожие

Immobilization of bioluminescent systems and their applications [Text] / E. N. Esimbekova, V. A. Kratasyuk ; ed. A Tsuji [et al.] // Bioluminescence & Chemiluminescence: Progress and Perspectives : WORLD SCIENTIFIC PUBL CO PTE LTD, 2005. - 13th International Symposium on Bioluminescence and Chemiluminescence (AUG 02-06, 2004, Yokohama, JAPAN). - P. 237-240, DOI 10.1142/9789812702203_0055. - Cited References: 14 . - ISBN 981-256-118-8

РУБ Biochemical Research Methods + Biochemistry & Molecular Biology + Chemistry, Applied + Chemistry, Physical + Optics
Рубрики:
ACIDS

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

Доп.точки доступа:
Esimbekova, E.N.; Kratasyuk, V.A.; Tsuji, A \ed.\; Matsurnoto, M \ed.\; Maeda, M \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

Найти похожие

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

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

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

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

Найти похожие

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

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

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

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

Найти похожие

10.

Ni2+-zeolite/ferrosphere and Ni2+-silica/ferrosphere beads for magnetic affinity separation of histidine-tagged proteins / T. A. Vereshchagina [et al.] // Dalton Trans. - 2016. - Vol. 45, Is. 4. - P1582-1592, DOI 10.1039/c5dt03827h . - ISSN 1477-9226
Кл.слова (ненормированные):
Alkalinity -- Amino acids -- Chemical modification -- Fly ash -- Hydrothermal synthesis -- Ion exchange -- Magnetic separation -- Magnetism -- Proteins -- Silica -- Zeolites -- Conventional methods -- Core shell structure -- Green fluorescent protein -- Histidine-tagged proteins -- Hydrothermal treatments -- Magnetic affinity -- Mesoporous Silica -- Sorption capacities -- Nickel
Аннотация: Magnetic Ni2+-zeolite/ferrosphere and Ni2+-silica/ferrosphere beads (Ni-ferrosphere beads - NFB) of a core-shell structure were synthesized starting from coal fly ash ferrospheres having diameters in the range of 0.063-0.050 mm. The strategy of NFB fabrication is an oriented chemical modification of the outer surface preserving the magnetic core of parent beads with the formation of micro-mesoporous coverings. Two routes of ferrosphere modification were realized, such as (i) hydrothermal treatment in an alkaline medium resulting in a NaP zeolite layer and (ii) synthesis of micro-mesoporous silica on the glass surface using conventional methods. Immobilization of Ni2+ ions in the siliceous porous shell of the magnetic beads was carried out via (i) the ion exchange of Na+ for Ni2+ in the zeolite layer or (ii) deposition of NiO clusters in the zeolite and silica pores. The final NFB were tested for affinity in magnetic separation of the histidine-tagged green fluorescent protein (GFP) directly from a cell lysate. Results pointed to the high affinity of the magnetic beads towards the protein in the presence of 10 mM EDTA. The sorption capacity of the ferrosphere-based Ni-beads with respect to GFP was in the range 1.5-5.7 mg cm-3. © The Royal Society of Chemistry.

Scopus,
WOS
Держатели документа:
Institute of Chemistry and Chemical Technology SB RAS, 50/24 Akademgorodok, Krasnoyarsk, Russian Federation
Institute of Biophysics SB RAS, 50/50 Akademgorodok, Krasnoyarsk, Russian Federation
Siberian Federal University, 79 Svobodnyi Avenue, Krasnoyarsk, Russian Federation

Доп.точки доступа:
Vereshchagina, T. A.; Fedorchak, M. A.; Sharonova, O. M.; Fomenko, E. V.; Shishkina, N. N.; Zhizhaev, A. M.; Kudryavtsev, A. N.; Frank, L. A.; Anshits, A. G.

Найти похожие

11.

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

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

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

Найти похожие

12.

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

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

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

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

Найти похожие

13.

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.

Scopus,
Смотреть статью,
WOS
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.

Найти похожие

14.

The Ca2+-Regulated Photoprotein Obelin as a Target for the RNA Aptamer Selection / V. V. Krasitskaya [et al.] // Russ. J. Bioorg. Chem. - 2018. - Vol. 44, Is. 3. - P296-301, DOI 10.1134/S1068162018030093 . - ISSN 1068-1620
Кл.слова (ненормированные):
2'-fluoro-RNA -- in vitro selection -- RNA aptamers -- Са2+-regulated photoprotein obelin
Аннотация: A variant of the Ca2+-regulated photoprotein obelin elongated with a hexahistidine peptide from the N-terminus was developed and studied. After immobilization on a metal-affine sorbent, the hybrid protein was applied as a target for the in vitro selection of RNA aptamers. According to the data of bioluminescent solid-phase microanalysis, the selection was shown to enrich the RNA library with obelin-affine molecules. © 2018, Pleiades Publishing, Ltd.

Scopus,
Смотреть статью,
WOS
Держатели документа:
Institute of Biophysics Siberian Branch, Russian Academy of Sciences, FRC Krasnoyarsk Science Center, Krasnoyarsk, Russian Federation
Institute of Chemical Biology and Fundamental Medicine, Siberian Branch, Russian Academy of Sciences, Novosibirsk, Russian Federation

Доп.точки доступа:
Krasitskaya, V. V.; Davydova, A. S.; Vorobjeva, M. A.; Frank, L. A.

Найти похожие

15.

Postglacial Colonization of the North European Seas by Pacific Fishes and Lamprey / A. A. Makhrov, D. L. Lajus // Contemp. Probl. Ecol. - 2018. - Vol. 11, Is. 3. - P247-258, DOI 10.1134/S1995425518030071. - Cited References:134. - This work was supported by Russian Science Foundation, project no. 16-14-10001. . - ISSN 1995-4255. - ISSN 1995-4263

РУБ Ecology
Рубрики:
MULTIPLE GLACIAL REFUGIA
   GENETIC DIFFERENTIATION
   SPECIES COMPLEX
   1956
Кл.слова (ненормированные):
Arctic Ocean -- zoogeography -- phylogeography -- fish -- lamprey -- evolution -- immobilization
Аннотация: A critical analysis of literature data on the distribution, morphology, and phylogeography of the Arctic lamprey (Lethenteron camtschaticum) and five species of marine and anadromous fish such as navaga (Eleginus navaga), pollock (Theragra chalcogramma), rainbow smelt (Osmerus mordax dentex), Pacific herring (Clupea pallasii), and pond smelt (Hypomesus olidus) has been performed. The results show that all these species have colonized Northern European seas, distributing along the Arctic coastline of Eurasia after the glacier retreat. The reasons that the dispersal of these species in the Atlantic Ocean may be impeded (preference for a cold environment, competition, and decrease of the evolutionary potential) are discussed.

WOS,
Смотреть статью,
Scopus
Держатели документа:
Russian Acad Sci, Severtsov Inst Ecol & Evolut, Moscow 119071, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
St Petersburg State Univ, St Petersburg 199178, Russia.

Доп.точки доступа:
Makhrov, A. A.; Lajus, D. L.; Russian Science Foundation [16-14-10001]

Найти похожие

16.

Phylogeny of Salmonoid Fishes (Salmonoidei) Based on mtDNA COI Gene Sequences (Barcoding) / V. S. Artamonova [et al.] // Contemp. Probl. Ecol. - 2018. - Vol. 11, Is. 3. - P271-285, DOI 10.1134/S1995425518030022. - Cited References:102. - We are very grateful to colleagues who helped collect samples: E.G. Berestovskii, I.N. Bolotov, E.A. Borovikova, I.V. Vikhrev, L.A. Glushchenko, V.V. Ignatenko, D.P. Karabanov, A.P. Novoselov, V.M. Spitsyn, V.A. Shirokov, and I.L. Shchurov; employees of Trout Hatchery "Adler", the Federal Breeding and Genetic Center for Fish Culture, and Vygsky and Kemsky fish hatcheries; and residents of Barabash-Levada, Len-lu, and Chupa settlements. We also thank S.S. Alekseev for identifying sharp-snouted and blunt-snouted lenoks. This work was supported by the Russian Science Foundation, project no. 16-14-10001. . - ISSN 1995-4255. - ISSN 1995-4263

РУБ Ecology
Рубрики:
MOLECULAR DATING ANALYSIS
GROWTH-HORMONE INTRONS
SALMONIFORMES
Кл.слова (ненормированные):
evolution -- network -- molecular clock -- amino acid sequence -- reproductive -- isolation -- immobilization -- fishes
Аннотация: We have analyzed the partial sequences of the mitochondrial COI gene along with the amino acid sequences of cytochrome oxidase subunit I, encoded by this gene region, in representatives of 11 genera of salmonoid fish. For amino acid sequences, two alternative networks are constructed with outgroups represented by either Esocoidei or Osmeroidei as the supposed ancestral groups. This way, Osmeroidei appear to be closer to the salmonoid fish than Esocoidei, and their presence in the network as an outgroup explains the available data on the morphology and karyology of salmonoids much better. A number of the results of this study are fundamentally new. In particular, the slowing down of the molecular evolution of the grayling (Thymallidae) is shown. We conclude that the charr (Salvelinus) is one of the modern genera of salmonoids closest to their ancestor. The hypothesis of the phylogenetic proximity of the genera Brachymystax, Hucho, and Salmo has been confirmed. We also discuss the possibility that it is namely the changes in the amino acid sequence of cytochrome oxidase subunit I that lead to postzygotic reproductive isolation between taxa.

WOS,
Смотреть статью,
Scopus
Держатели документа:
Russian Acad Sci, Severtsov Inst Ecol & Evolut, Moscow 119071, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Artamonova, V. S.; Kolmakova, O. V.; Kirillova, E. A.; Makhrov, A. A.; Russian Science Foundation [16-14-10001]

Найти похожие

17.

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.

WOS,
Смотреть статью,
Scopus
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.

Найти похожие

18.

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.

WOS,
Смотреть статью
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]

Найти похожие

19.

Polysaccharide-coated iron oxide nanoparticles: Synthesis, properties, surface modification / S. V. Stolyar, V. V. Krasitskaya, L. A. Frank [et al.] // Mater Lett. - 2021. - Vol. 284. - Ст. 128920, DOI 10.1016/j.matlet.2020.128920 . - ISSN 0167-577X
Кл.слова (ненормированные):
Biomaterials -- Magnetic materials -- Nanoparticles -- Polysaccharide -- Iron oxides -- Magnetite -- Magnetite nanoparticles -- Molecules -- Polysaccharides -- Synthesis (chemical) -- Arabinogalactan -- Bioanalytical systems -- Covalent immobilization -- Iron oxide nanoparticle -- Magnetic nanoparticles
Аннотация: In this work, magnetite nanoparticles coated with polysaccharides were synthesized. Arabinogalactan and chitosan were used as polysaccharides. The possibilities of immobilization of biospecific molecules on the surface of the obtained composites were studied. Experiments on covalent immobilization of biospecific molecules on magnetic nanoparticles coated with a polysaccharide showed a high density of immobilized molecules. This suggests the use of such materials in bioanalytical systems or as affinity sorbents. © 2020 Elsevier B.V.

Scopus
Держатели документа:
Krasnoyarsk Scientific Center, Federal Research Center KSC SB RAS, Krasnoyarsk, Russian Federation
Kirensky Institute of Physics, Federal Research Center KSC SB RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Federal Research Center KSC SB RAS, Krasnoyarsk, Russian Federation
Astrakhan State University, Astrakhan, Russian Federation
University of Al-qasim Green, College of Biotechnology, Iraq

Доп.точки доступа:
Stolyar, S. V.; Krasitskaya, V. V.; Frank, L. A.; Yaroslavtsev, R. N.; Chekanova, L. A.; Gerasimova, Y. V.; Volochaev, M. N.; Bairmani, M. S.; Velikanov, D. A.

Найти похожие

20.

Polysaccharide-coated iron oxide nanoparticles: Synthesis, properties, surface modification / S. V. Stolyar, V. V. Krasitskaya, L. A. Frank [et al.] // Mater. Lett. - 2021. - Vol. 284. - Ст. 128920, DOI 10.1016/j.matlet.2020.128920. - Cited References:12. - The reported study was carried out with the financial support of the Russian Foundation for Fundamental Research, the Government of the Krasnoyarsk Territory, the Krasnoyarsk Territory Fund for Support of Scientific and Technical Activity in the framework of scientific Project No. 18-43-243003. This work was supported by the Council of the President of the Russian Federation for State Support of Young Scientists and Leading Scientific Schools (project no. MK-1263.2020.3). . - ISSN 0167-577X. - ISSN 1873-4979

РУБ Materials Science, Multidisciplinary + Physics, Applied

Кл.слова (ненормированные):
Nanoparticles -- Biomaterials -- Magnetic materials -- Polysaccharide
Аннотация: In this work, magnetite nanoparticles coated with polysaccharides were synthesized. Arabinogalactan and chitosan were used as polysaccharides. The possibilities of immobilization of biospecific molecules on the surface of the obtained composites were studied. Experiments on covalent immobilization of biospecific molecules on magnetic nanoparticles coated with a polysaccharide showed a high density of immobilized molecules. This suggests the use of such materials in bioanalytical systems or as affinity sorbents. (c) 2020 Elsevier B.V. All rights reserved.

WOS
Держатели документа:
RAS, Krasnoyarsk Sci Ctr, Fed Res Ctr, KSC,SB, Krasnoyarsk, Russia.
RAS, Kirensky Inst Phys, Fed Res Ctr, KSC,SB, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.
RAS, Inst Biophys, Fed Res Ctr, KSC,SB, Krasnoyarsk, Russia.
Astrakhan State Univ, Astrakhan, Russia.
Univ Al Qasim Green, Coll Biotechnol, Al Qasim, Iraq.

Доп.точки доступа:
Stolyar, S. V.; Krasitskaya, V. V.; Frank, L. A.; Yaroslavtsev, R. N.; Chekanova, L. A.; Gerasimova, Y. V.; Volochaev, M. N.; Bairmani, M. Sh.; Velikanov, D. A.; Russian Foundation for Fundamental ResearchRussian Foundation for Basic Research (RFBR); Government of the Krasnoyarsk Territory; Krasnoyarsk Territory Fund [18-43-243003]; Council of the President of the Russian Federation for State Support of Young Scientists and Leading Scientific SchoolsLeading Scientific Schools Program [MK-1263.2020.3]

Найти похожие

Тематический навигатор

Другие библиотеки

Библиотека института физики

Центральная научная библиотека КНЦ СО РАН

Библиотека института химии и химический технологии

Библиотека института вычислительного моделирования

Библиотека института леса

Библиотека СФУ

Краевая научная библиотека

© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)