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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gitelson J.I., V B., Grigoriev A.I., Lisovsky G.M., Manukovsky N.S., Sinyak Y.u.E., Ushakova S.A.
Заглавие : Biological-physical-chemical aspects of a human life support system for a lunar base
Место публикации : Acta Astronautica. - 1995. - Vol. 37, Is. C. - С. 385-394. - ISSN 00945765 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., TROFIMOV K.P., VYSOTSKII E.S.
Заглавие : PHYSICOCHEMICAL PROPERTIES OF A PHOTOPROTEIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 10. - С. 1020-1027. - 8. - ISSN 0006-2979
Примечания : Cited References: 36
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
CA-2+
INDICATORS
PROTEIN
BINDING
PURIFICATION
EXTRACTION
Ключевые слова (''Своб.индексиров.''): 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
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Petushkov V.N., Gibson B.G., Lee J.
Заглавие : Properties of recombinant fluorescent proteins from Photobacterium leiognathi and their interaction with luciferase intermediates
Место публикации : Biochemistry. - 1995. - Vol. 34, Is. 10. - С. 3300-3309. - ISSN 00062960 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Kolmakov V.I.
Заглавие : Role of Microcystis aeruginosa passing through the digestive tracts of filter-feeding animals in eutrophic water reservoirs (review)
Колич.характеристики :10 с
Коллективы : Federal Targeted Program "Scientific and Scientific-Pedagogical Personnel of an Innovative Russia" [16.740.11.0484]
Место публикации : Contemp. Probl. Ecol.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2014. - Vol. 7, Is. 4. - С. 455-464. - ISSN 1995-4255, DOI 10.1134/S1995425514040052. - ISSN 1995-4263
Примечания : 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).
Предметные 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
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ronzhin N. O., Posokhina E. D., Mikhlina E. V., Simunin M. M., Nemtsev I. V., Ryzhkov I. I., Bondar V. S.
Заглавие : Production of a Composite Based on Alumina Nanofibers and Detonation Nanodiamonds for Creating Phenol Indication Systems
Место публикации : Dokl. Chem.: Pleiades Publishing, 2019. - Vol. 489, Is. 1. - С. 267-271. - ISSN 00125008 (ISSN), DOI 10.1134/S001250081911003X
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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ronzhin N. O., Posokhina E. D., Mikhlina E. V., Simunin M. M., Nemtsev I. V., Ryzhkov I. I., Bondar V. S.
Заглавие : Production of a Composite Based on Alumina Nanofibers and Detonation Nanodiamonds for Creating Phenol Indication Systems
Колич.характеристики :5 с
Коллективы : Russian Foundation for Basic ResearchRussian Foundation for Basic Research (RFBR) [18-29-19078 mk]
Место публикации : Dokl. Chem.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2019. - Vol. 489. - С. 267-271. - ISSN 0012-5008, DOI 10.1134/S001250081911003X. - ISSN 1608-3113(eISSN)
Примечания : Cited References:13. - This work was supported by the Russian Foundation for Basic Research (project no. 18-29-19078 mk).
Предметные 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
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Ronzhin N. O., Mogilnaya O. A., Artemenko K. S., Posokhina E. D., Bondar V. S.
Заглавие : Extracellular Oxidases of Basidiomycete Neonothopanus nambi: Isolation and Some Properties
Колич.характеристики :5 с
Место публикации : Dokl. Biochem. Biophys.: MAIK NAUKA/INTERPERIODICA/SPRINGER, 2020. - Vol. 490, Is. 1. - С. 38-42. - ISSN 1607-6729, DOI 10.1134/S1607672920010135. - ISSN 1608-3091(eISSN)
Примечания : Cited References:15
Предметные рубрики: PEROXIDASE-ACTIVITY
LIGHT-EMISSION
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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Mogilnaya, Olga, Ronzhin, Nikita, Posokhina, Ekaterina, Bondar, Vladimir
Заглавие : Extracellular Oxidase from the Neonothopanus nambi Fungus as a Promising Enzyme for Analytical Applications
Колич.характеристики :10 с
Коллективы : [0356-2019-0022]
Место публикации : Protein J.: SPRINGER, 2021. - Article in press. - ISSN 1572-3887, DOI 10.1007/s10930-021-10010-z. - ISSN 1573-4943(eISSN)
Примечания : 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.
Предметные рубрики: ARYL-ALCOHOL OXIDASE
GLUCOSE-OXIDASE
PEROXIDASES
MECHANISM
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.
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