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1.


   
    Role of Microcystis aeruginosa passing through the digestive tracts of filter-feeding animals in eutrophic water reservoirs (review) [Text] / V. I. Kolmakov // Contemp. Probl. Ecol. - 2014. - Vol. 7, Is. 4. - P455-464, DOI 10.1134/S1995425514040052. - Cited References: 100. - This study was performed at the Siberian Federal University (project "Ecological and Biophysical Mechanisms of the Quality of Production in the Aquatic Ecosystems of the Yenisei River Basin") within the framework of the State Requirement of the Ministry of Education and Science of the Russian Federation for the provision of services (performance of activities), as well as by the Federal Targeted Program "Scientific and Scientific-Pedagogical Personnel of an Innovative Russia" (project no. 16.740.11.0484). . - ISSN 1995-4255. - ISSN 1995-4263
РУБ Ecology
Рубрики:
CARP HYPOPHTHALMICHTHYS-MOLITRIX
   TILAPIA OREOCHROMIS-NILOTICUS

   MUSSEL DREISSENA-POLYMORPHA

   BLOOM-FORMING CYANOBACTERIUM

   VIABLE GUT PASSAGE

   LOW-NUTRIENT LAKES

   ZEBRA MUSSEL

   PHYTOPLANKTIVOROUS FISH

   SELECTIVE FILTRATION

   ALGAL COMPOSITION

Кл.слова (ненормированные):
Microcystis aeruginosa -- viable gut passage -- water bloom -- planktivorous fish -- daphnia -- bivalves -- eutrophic reservoirs
Аннотация: The foreign and Russian literature devoted to studying the effect of enhancing the growth of colonies of the cyanobacterium Microcystis aeruginosa Kutz em. Elenk. after their passage in a viable state through the digestive tract of filter-feeding aquatic animals (planktivorous fish, daphnia, and bivalves) has been analyzed. The main mechanisms of this effect are considered. Its role in the functioning of eutrophic reservoirs is discussed. The prospects and the need for further studies of the effect of enhancing Microcyctis growth after its viable passage through the digestive tracts of filter-feeding animals are shown for the development of a complete theory of the functioning of aquatic ecosystems.

WOS
Держатели документа:
[Kolmakov, V. I.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
[Kolmakov, V. I.] Russian Acad Sci, Siberian Branch, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Kolmakov, V.I.; Federal Targeted Program "Scientific and Scientific-Pedagogical Personnel of an Innovative Russia" [16.740.11.0484]

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2.


   
    Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates / V. N. Petushkov, B. G. Gibson, J. Lee // Biochemistry. - 1995. - Vol. 34, Is. 10. - P3300-3309 . - ISSN 0006-2960
Кл.слова (ненормированные):
luciferase -- recombinant protein -- article -- ligand binding -- nonhuman -- priority journal -- protein isolation -- protein protein interaction -- protein stability -- vibrionaceae -- Bacterial Proteins -- Binding Sites -- Carrier Proteins -- Circular Dichroism -- Flavin Mononucleotide -- Fluorescence Polarization -- Genes, Bacterial -- Kinetics -- Ligands -- Luciferase -- Luminescence -- Molecular Sequence Data -- Photobacterium -- Recombinant Proteins -- Spectrophotometry -- Support, U.S. Gov't, P.H.S. -- Photobacterium leiognathi -- Vibrionaceae
Аннотация: Ligand binding and luciferase interaction properties of the recombinant protein corresponding to the lumazine protein gene (EMBL X56534) of Photobacterium leiognathi have been determined by fluorescence dynamics, circular dichroism, gel filtration, and SDS-PAGE. Scatchard analysis of a fluorescence titration shows that the apoprotein possess one binding site, and at 30В°C the KdS (?M) are as follows: 6,7-dimethyl-8-ribityllumazine, 0.26; riboflavin, 0.53; and much more weakly bound FMN, 30. All holoproteins are highly fluorescent and have absorption spectra distinct from each other and from the free ligands. The longest wavelength absorption maxima are, respectively (nm, 2В°C), 420,463, and 458. Ligand binding produces no change in the far-UV circular dichroism; all have mean residual ellipticity at 210 nm of -6500 deg cm2 dmol-1, the same as the native protein. However, in the bioluminescence reaction only the lumazine holoprotein shows a bioluminescence effect. Fluorescence emission anisotropy decay was used to establish that none of these holoproteins complexed with native luciferase and that the lumazine protein alone formed a 1:1 complex with the luciferase hydroxyflavin fluorescent transient and the luciferase peroxyflavin intermediates, revealed by a dominant channel of anisotropy loss, with rotational correlation time of 2.5 ns, and attributed to excitation transfer from the luciferase flavin donor to the acceptor, the lumazine ligand. The complex stability was sufficient to allow its isolation by FPLC gel filtration and verification by SDS-PAGE. These methods also confirmed the absence of interaction of the holoflavoproteins.

Scopus
Держатели документа:
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, United States
Institute of Biophysics, Academy of Sciences of Russia (Siberian Branch), 660036 Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Gibson, B.G.; Lee, J.

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3.


   
    Production of a Composite Based on Alumina Nanofibers and Detonation Nanodiamonds for Creating Phenol Indication Systems / N. O. Ronzhin, E. D. Posokhina, E. V. Mikhlina [et al.] // Dokl. Chem. - 2019. - Vol. 489, Is. 1. - P267-271, DOI 10.1134/S001250081911003X . - ISSN 0012-5008
Аннотация: Abstract: A composite of alumina nanofibers (ANF) and modified detonation nanodiamonds (MDND) was produced by mixing aqueous suspensions of the components in a weight ratio of 5 : 1 with subsequent incubation of the mixture for 15 min at 32°C. It was assumed that the formation of the composite is ensured by the difference of the zeta potentials of the components, which is negative for MDND and positive for ANF. Vacuum filtration of the mixture through a fluoroplastic filter (pore diameter 0.6 ?m) formed disks 40 mm in diameter, which were then heat-treated at 300°C to impart structural stability to the composite. Scanning electron microscopy detected that the obtained composite has a network structure, in which MDND particles are distributed over the surface of ANF. It was determined that the MDND particles incorporated in the composite catalyze the phenol–4-aminoantipyrine–H2O2 oxidative azo coupling reaction to form a colored product (quinoneimine). The applicability of the composite to repeated phenol detection in aqueous samples was demonstrated. © 2019, Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, AkademgorodokKrasnoyarsk, 660036, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation
Institute of Computational Modeling, Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, AkademgorodokKrasnoyarsk, 660036, Russian Federation
Krasnoyarsk Scientific Center, Siberian Branch, Russian Academy of Sciences, AkademgorodokKrasnoyarsk, 660036, Russian Federation

Доп.точки доступа:
Ronzhin, N. O.; Posokhina, E. D.; Mikhlina, E. V.; Simunin, M. M.; Nemtsev, I. V.; Ryzhkov, I. I.; Bondar, V. S.

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4.


   
    Production of a Composite Based on Alumina Nanofibers and Detonation Nanodiamonds for Creating Phenol Indication Systems / N. O. Ronzhin, E. D. Posokhina, E. V. Mikhlina [et al.] // Dokl. Chem. - 2019. - Vol. 489. - P267-271, DOI 10.1134/S001250081911003X. - Cited References:13. - This work was supported by the Russian Foundation for Basic Research (project no. 18-29-19078 mk). . - ISSN 0012-5008. - ISSN 1608-3113
РУБ Chemistry, Multidisciplinary
Рубрики:
NANOPARTICLES
   GRAPHENE

Аннотация: A composite of alumina nanofibers (ANF) and modified detonation nanodiamonds (MDND) was produced by mixing aqueous suspensions of the components in a weight ratio of 5 : 1 with subsequent incubation of the mixture for 15 min at 32 degrees C. It was assumed that the formation of the composite is ensured by the difference of the zeta potentials of the components, which is negative for MDND and positive for ANF. Vacuum filtration of the mixture through a fluoroplastic filter (pore diameter 0.6 mu m) formed disks 40 mm in diameter, which were then heat-treated at 300 degrees C to impart structural stability to the composite. Scanning electron microscopy detected that the obtained composite has a network structure, in which MDND particles are distributed over the surface of ANF. It was determined that the MDND particles incorporated in the composite catalyze the phenol-4-aminoantipyrine-H2O2 oxidative azo coupling reaction to form a colored product (quinoneimine). The applicability of the composite to repeated phenol detection in aqueous samples was demonstrated.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Inst Biophys, Krasnoyarsk 660036, Russia.
Siberian Fed Univ, Krasnoyarsk 660041, Russia.
Russian Acad Sci, Siberian Branch, Inst Computat Modeling, Krasnoyarsk Sci Ctr, Krasnoyarsk 660036, Russia.
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci Ctr, Krasnoyarsk 660036, Russia.

Доп.точки доступа:
Ronzhin, N. O.; Posokhina, E. D.; Mikhlina, E. V.; Simunin, M. M.; Nemtsev, I. V.; Ryzhkov, I. I.; Bondar, V. S.; Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-29-19078 mk]

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5.


   
    PHYSICOCHEMICAL PROPERTIES OF A PHOTOPROTEIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA [Text] / V. S. BONDAR, K. P. TROFIMOV, E. S. VYSOTSKII // Biochem.-Moscow. - 1992. - Vol. 57, Is. 10. - P1020-1027. - Cited References: 36 . - 8. - ISSN 0006-2979
РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP

   BEROE-OVATA

   AEQUORIN

   CA-2+

   INDICATORS

   PROTEIN

   BINDING

   PURIFICATION

   EXTRACTION

Кл.слова (ненормированные):
BIOLUMINESCENCE -- CA2+-ACTIVATED PHOTOPROTEIN -- OBELIN -- CHROMATOGRAPHY -- CALCIUM
Аннотация: The photoprotein obelin was isolated and purified to homogeneity (as indicated by sodium dodecyl sulfate polyacrylamide gel electrophoresis) from hydroids of Obelia longissima by gel filtration on Sephadex G-75 fine, ion exchange chromatography on Polysil CA-300 (10 mum), hydrophobic chromatography on Phenyl-Sepharose CL-4B, gel filtration on Sephacryl S-200 superfine, ion exchange chromatography on a Mono Q column at pH 7.0, chromatofocusing on a Mono P column (pH gradient 6.0-4.0), and ion exchange chromatography on a Mono Q column at pH 5.5, 8.8, and 7.0. The molecular weight of the native protein was 30 kD, and that measured in the presence of SDS was 19.8 kD. The specific activity of obelin is 4.9.10(15) quanta/mg protein, pseudo-first-order constant of bioluminescence decay 4 sec-1, and quantum yield 0.16 The range of measurable Ca2+ concentrations is 10(-7) to 10(-5) M. The luminescence spectrum of obelin peaks at 469 nm, and the fluorescence emission maximum of the discharged protein is at 455 nm. The optimum pH for luminescence is between 9.0 and 10.5. The molecular ionization constants are pK1 6.8 and pK2 12.2, and the ionization constants for the active site are pK1 9.1 and pK2 10.2
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; TROFIMOV, K.P.; VYSOTSKII, E.S.

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6.


   
    Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties / N. O. Ronzhin, O. A. Mogilnaya, K. S. Artemenko [et al.] // Dokl. Biochem. Biophys. - 2020. - Vol. 490, Is. 1. - P38-42, DOI 10.1134/S1607672920010135. - Cited References:15 . - ISSN 1607-6729. - ISSN 1608-3091
РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
PEROXIDASE-ACTIVITY
   LIGHT-EMISSION

Кл.слова (ненормированные):
extracellular oxidases -- basidiomycete Neonothopanus nambi -- beta-glucosidase -- gel-filtration chromatography -- veratryl alcohol -- phenol -- FAD
Аннотация: Using the original technique of treating biomass with beta-glucosidase, a pool of extracellular fungal enzymes was obtained for the first time from the mycelium of basidiomycete Neonothopanus nambi. Two protein fractions containing enzymes with oxidase activity were isolated from the extract by gel-filtration chromatography and conventionally called F1 and F2. Enzyme F1 has a native molecular weight of 80-85 kDa and does not contain chromophore components; however, it catalyzes the oxidation of veratryl alcohol with K-m = 0.52 mM. Probably, this enzyme is an alcohol oxidase. Enzyme F2 with a native molecular weight of approximately 60 kDa is a FAD-containing protein. It catalyzes the cooxidation of phenol with 4-aminoantipyrine without the addition of exogenous hydrogen peroxide, which distinguishes it from the known peroxidases. It was assumed that this enzyme may be a mixed-function oxidase. F2 oxidase has K-m value 0.27 mM for phenol. The temperature optimums for oxidases F1 and F2 are 22-35 and 55-70 degrees C, and pH optimums are 6 and 5, respectively.

WOS
Держатели документа:
Russian Acad Sci, Siberian Branch, Krasnoyarsk Sci, Inst Biophys,Fed Res Ctr, Krasnoyarsk, Russia.
Siberian Fed Univ, Krasnoyarsk, Russia.

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

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7.


   
    Extracellular Oxidase from the Neonothopanus nambi Fungus as a Promising Enzyme for Analytical Applications / O. Mogilnaya, N. Ronzhin, E. Posokhina, V. Bondar // Protein J. - 2021, DOI 10.1007/s10930-021-10010-z. - Cited References:39. - This work was supported by the state budget allocated to the fundamental research at the Russian Academy of Sciences, Project No. 0356-2019-0022. . - Article in press. - ISSN 1572-3887. - ISSN 1573-4943
РУБ Biochemistry & Molecular Biology
Рубрики:
ARYL-ALCOHOL OXIDASE
   GLUCOSE-OXIDASE

   PEROXIDASES

   MECHANISM

Кл.слова (ненормированные):
Extracellular oxidase -- Flavoprotein -- Fungi -- Phenol
Аннотация: The extracellular enzyme with oxidase function was extracted from the Neonothopanus nambi luminescent fungus by using mild processing of mycelium with beta-glucosidase and then isolated by gel-filtration chromatography. The extracted enzyme is found to be a FAD-containing protein, catalyzing phenol co-oxidation with 4-aminoantipyrine without addition of H2O2, which distinguishes it from peroxidases. This fact allowed us to assume that this enzyme may be a mixed-function oxidase. According to gel-filtration chromatography and SDS-PAGE, the oxidase has molecular weight of 60 kDa. The enzyme exhibits maximum activity at 55-70 degrees C and pH 5.0. Kinetic parameters K-m and V-max of the oxidase for phenol were 0.21 mM and 0.40 mu M min(-1). We suggest that the extracted enzyme can be useful to develop a simplified biosensor for colorimetric detection of phenol in aqueous media, which does not require using hydrogen peroxide.

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

Доп.точки доступа:
Mogilnaya, Olga; Ronzhin, Nikita; Posokhina, Ekaterina; Bondar, Vladimir; [0356-2019-0022]

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8.


   
    Biological-physical-chemical aspects of a human life support system for a lunar base / J. I. Gitelson [et al.] // Acta Astronautica. - 1995. - Vol. 37, Is. C. - P385-394 . - ISSN 0094-5765
Кл.слова (ненормированные):
animal -- aquaculture -- article -- biomass -- construction work and architectural phenomena -- Cyprinodontiformes -- filtration -- growth, development and aging -- human -- microbiology -- microclimate -- moon -- nutritional value -- photoperiodicity -- plant -- space flight -- standard -- Tilapia -- waste management -- water management -- wheat -- Animals -- Aquaculture -- Biomass -- Cyprinodontiformes -- Ecological Systems, Closed -- Facility Design and Construction -- Filtration -- Humans -- Life Support Systems -- Moon -- Nutritive Value -- Photoperiod -- Plants, Edible -- Space Flight -- Tilapia -- Triticum -- Waste Management -- Water Microbiology -- Water Purification
Аннотация: To create a life support system based on biological and physical-chemical processes is the optimum solution providing full-valued condidtions for existence and efficient work of people at a lunar base. Long-standing experinece in experimental research or closed ecosystems and their components allows us to suggest a realistic functional structure of the lunar base and to estimate qualitatively its parameters. The original restrictions are as follows: 1) the basic source of energy to support the biological processes has to be the solar radiation; 2) the initial amount of basic biological elelments forming the turnover of substances (C, O, H, P, K, N) has to be delivered from Earth; 3). Moon materials are not to be used in the biological turnover inside the base; 4) the base is to supply the crew fully with atmosphere and water, and with 90% (A scenario) or 40% (B scenario) of food. Experimental data about the plant productivity under the "Moon" rhythm of light and darkness allow us to suggest that the A scenario requires per one human: plant area - 40 m2 irradiated during the lunar day by 250-300 W/m2 PAR producing 1250 g of dry biomass a terrestrial day; a heterotrophic component of "biological incineration" of inedible plant biomass (800 g/day) including the aquaculture of fish to produce animal products and contaminating the environment less than birds and mammals, and the culture of edible mushrooms; a component of physical-chemical correction for the LSS envi ronment including the subsystems of: deep oxidation of organic impurities in the atmosphere and of water, organic wastes of human activity and that biological components (420 g/day) Co2 concentration in "Moon" nights, damping O2 in "Moon" days, etc. The stock of presotred or delivered from Earth substances (food additions, seeds, etc.) to be involved in biological turnover is to be about 50 kg/year per man. Increase of the mass of prestored substances per man up to 220 kg/year would reduce twice the plant area and consumed amount of radiant energy to exclude the components of "biological incineration" and physical-chemical destruction of organic wastes. В© 1995.

Scopus
Держатели документа:
Institute of Biophysics (Russian Academy of Sciences, Siberian Branch) Krasnoyarsk, Russian Federation
Ruhr-University of Bochum, C.E.B.A.S. Center of Excellence., Bochum, Germany
Institute of Medical-Biological Problems, Moscow, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gitelson, J.I.; V, B.; Grigoriev, A.I.; Lisovsky, G.M.; Manukovsky, N.S.; Sinyak, Y.u.E.; Ushakova, S.A.

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