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1.


   
    241Am distribution in the biomass of freshwater macrophytes / T. A. Zotina [et al.] // Doklady Biological Sciences. - 2008. - Vol. 421, Is. 1. - P254-256, DOI 10.1134/S0012496608040108 . - ISSN 0012-4966
Кл.слова (ненормированные):
americium -- carbohydrate -- cellulose -- lipid -- nitrogen -- polysaccharide -- vegetable protein -- article -- biomass -- Bryopsida -- cell membrane -- cell wall -- chemistry -- cytoplasm -- food chain -- growth, development and aging -- Hydrocharitaceae -- metabolism -- Americium -- Biomass -- Bryopsida -- Carbohydrates -- Cell Membrane -- Cell Wall -- Cellulose -- Cytoplasm -- Food Chain -- Hydrocharitaceae -- Lipids -- Nitrogen -- Plant Proteins -- Polysaccharides

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

Доп.точки доступа:
Zotina, T.A.; Kalachova, G.S.; Bolsunovsky, A.Ya.; Degermendzhy, A.G.

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2.


   
    Characteristics of proteins synthesized by hydrogen-oxidizing microorganisms / T. G. Volova, V. A. Barashkov // Applied Biochemistry and Microbiology. - 2010. - Vol. 46, Is. 6. - P574-579, DOI 10.1134/S0003683810060037 . - ISSN 0003-6838
Кл.слова (ненормированные):
Animalia -- Bacteria (microorganisms) -- Cupriavidus necator -- Pseudomonas carboxydohydrogena
Аннотация: The study was conducted to determine the biological value of proteins synthesized by hydrogen-oxidizing microorganisms-the hydrogen bacteria Alcaligenes eutrophus Z1 and Ralstonia eutropha B5786 and the CO-resistant strain of carboxydobacterium Seliberia carboxydohydrogena Z1062. Based on a number of significant parameters characterizing the biological value of a product, the proteins of hydrogen-oxidizing microorganisms have been found to occupy an intermediate position between traditional animal and plant proteins. The high total protein in biomass of these microorganisms, their complete amino acid content, and availability to proteolytic enzymes allow for us to consider these microorganisms as potential protein producers. В© 2010 Pleiades Publishing, Ltd.

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

Доп.точки доступа:
Volova, T.G.; Barashkov, V.A.

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3.


   
    Luminous bacteria as potential producers of resorbed polyhydroxyalkanoate polyesters / A. N. Boyandin [et al.] // Doklady Biochemistry and Biophysics. - 2007. - Vol. 416, Is. 1-6. - P248-251, DOI 10.1134/S1607672907050067 . - ISSN 1607-6729
Кл.слова (ненормированные):
photoprotein -- polyester -- polyhydroxyalkanoic acid -- article -- bacterium -- chemistry -- chemoluminescence -- classification -- genetic procedures -- genetics -- metabolism -- Photobacterium -- phylogeny -- time -- Bacteria -- Biosensing Techniques -- Chemiluminescent Measurements -- Luminescent Proteins -- Photobacterium -- Phylogeny -- Polyesters -- Polyhydroxyalkanoates -- Time Factors -- Bacteria (microorganisms)

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

Доп.точки доступа:
Boyandin, A.N.; Kalacheva, G.S.; Rodicheva, E.K.; Volova, T.G.

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4.


   
    Biochemical fractionation and cellular distribution of americium and plutonium in the biomass of freshwater macrophytes / T. A. Zotina, G. S. Kalacheva, A. Y. Bolsunovsky // Journal of Radioanalytical and Nuclear Chemistry. - 2011. - Vol. 290, Is. 2. - P447-451, DOI 10.1007/s10967-011-1228-2 . - ISSN 0236-5731
Кл.слова (ненормированные):
238, 242Pu -- 241Am -- Carbohydrates -- Cellulose -- Fractionation -- Protein -- Submerged macrophyte -- americium 241 -- plutonium -- plutonium 238 -- plutonium 242 -- polysaccharide -- unclassified drug -- article -- bioaccumulation -- biomass -- cellular distribution -- Ceratophyllum demersum -- controlled study -- cytosol -- Elodea canadensis -- Fontinalis antipyretica -- fractionation -- freshwater species -- macrophyte -- moss -- Myriophyllum spicatum -- nonhuman -- plant cell -- radiation absorption -- radioactivity -- shoot
Аннотация: Accumulation of americium ( 241Am) and plutonium ( 238,242Pu) and their distribution in cell compartments and biochemical components of the biomass of freshwater aquatic plants Elodea canadensis, Ceratophyllum demersum and Myrioplyllum spicatum and aquatic moss Fontinalis antipyretica have been investigated in laboratory experiments. Americium and plutonium taken up from water by Elodea canadensis apical shoots were mainly absorbed by structural components of plant cells (90% for 241Am; 89% for 238Pu and 82-87% for 242Pu). About 10-18% of isotope activity was recorded in the cytosol fraction. The major concentration (76-92%) of americium was bound to cell wall cellulose-like polysaccharides of Elodea canadensis, Myriophyllum spicatum, Ceratophyllum demersum and Fontinalis antipyretica, 8-24% of americium activity was registered in the fraction of proteins and carbohydrates, and just a minor concentration (<1%) in the lipid fraction. The distribution of plutonium in the biomass fractions of Elodea was similar to that of americium. Hence, americium and plutonium had the highest affinity to cellulose-like polysaccharides of cell walls of freshwater submerged macrophytes. В© 2011 Akademiai Kiado, Budapest, Hungary.

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

Доп.точки доступа:
Zotina, T.A.; Kalacheva, G.S.; Bolsunovsky, A.Y.

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5.


   
    Comparative study of Thermoresistances' cellular mechanisms in representatives of the Gammarus lacustris Sars populations inhabiting Saline Lake Shira (Republic of Khakassia) and a fresh water body in the Cis-Baikal region / Z. M. Shatilina [et al.] // Doklady Biological Sciences. - 2010. - Vol. 434, Is. 1. - P359-362, DOI 10.1134/S0012496610050182 . - ISSN 0012-4966
Кл.слова (ненормированные):
antioxidant -- catalase -- fresh water -- heat shock protein 70 -- reactive oxygen metabolite -- sea water -- Amphipoda -- animal -- article -- biosynthesis -- comparative study -- ecosystem -- heat -- metabolism -- Russian Federation -- Amphipoda -- Animals -- Antioxidants -- Catalase -- Ecosystem -- Fresh Water -- Hot Temperature -- HSP70 Heat-Shock Proteins -- Reactive Oxygen Species -- Seawater -- Siberia -- Gammarus -- Gammarus lacustris

Scopus
Держатели документа:
Institute of Biology, Irkutsk State University, ul. Lenina 3, Irkutsk 664003, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation
Siberian Federal University, pr. Svobodnyi 79, Krasnoyarsk 660041, Russian Federation
Irkutsk State University, ul. Karla Marksa 1, Irkutsk 664003, Russian Federation
Baikal Research Centre, ul. Karla Marksa 5-10, Irkutsk 664003, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Shatilina, Z.M.; Gubanov, M.V.; Zadereev, E.S.; Pavlichenko, V.V.; Axenov-Gribanov, D.V.; Sapozhnikova, E.A.; Protopopova, M.V.; Bedulina, D.S.; Timofeyev, M.A.

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6.


   
    An ontogenetic approach to the assessment of plant resistance to stress factors based on the method of chlorophyll fluorescence induction. / T. V. Nesterenko, A. A. Tikhomirov // Doklady. Biochemistry and biophysics. - 2003. - Vol. 388. - P4-7 . - ISSN 1607-6729
Кл.слова (ненормированные):
chlorophyll -- adaptation -- aging -- article -- comparative study -- cucumber -- light -- metabolism -- methodology -- photostimulation -- photosynthesis -- physiology -- plant leaf -- radiation dose -- radiation exposure -- spectrofluorometry -- Adaptation, Physiological -- Aging -- Chlorophyll -- Cucumis sativus -- Light -- Photic Stimulation -- Photosynthetic Reaction Center Complex Proteins -- Plant Leaves -- Radiation Dosage -- Spectrometry, Fluorescence

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

Доп.точки доступа:
Nesterenko, T.V.; Tikhomirov, A.A.

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7.


   
    Perspectives of different type biological life support systems (BLSS) usage in space missions / S. I. Bartsev [et al.] // Acta Astronautica. - 1996. - Vol. 39, Is. 8. - P617-622, DOI 10.1016/S0094-5765(97)00012-X . - ISSN 0094-5765
Кл.слова (ненормированные):
article -- bacterium -- comparative study -- construction work and architectural phenomena -- environmental planning -- green alga -- human -- instrumentation -- mathematics -- microclimate -- moon -- plant -- quality of life -- space flight -- standard -- weightlessness -- Algae, Green -- Bacteria -- Ecological Systems, Closed -- Environment Design -- Environment, Controlled -- Facility Design and Construction -- Humans -- Life Support Systems -- Mathematics -- Moon -- Plants -- Quality of Life -- Space Flight -- Weightlessness -- Biology -- Life support systems (spacecraft) -- Spreadsheets -- Biological life support systems (BLSS) -- Lunar missions
Аннотация: In the paper an attempt is made to combine three important criteria of LSS comparison: minimum mass, maximum safety and maximum quality of life. Well-known types of BLSS were considered: with higher plant, higher plants and mushrooms, microalgae, and hydrogen-oxidizing bacteria. These BLSSs were compared in terms of "integrated" mass for the case of a vegetarian diet and a "normal" one (with animal proteins and fats). It was shown that the BLSS with higher plants and incineration of wastes becomes the best when the exploitation period is more than 1 yr. The dependence of higher plants' LSS structure on operation time was found. Comparison of BLSSs in terms of integral reliability (this criterion includes mass and quality of life criteria) for a lunar base scenario showed that BLSSs with higher plants are advantageous in reliability and comfort. This comparison was made for achieved level of technology of closing and for perspective one. В© 1997 Elsevier Science Ltd.

Scopus
Держатели документа:
Biophys. Inst. of SB RAS, Krasnoyarsk, 660036, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Bartsev, S.I.; Gitelson, J.I.; Lisovsky, G.M.; Mezhevikin, V.V.; Okhonin, V.A.

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8.


   
    Nucleotide sequence of part of Photobacterium leiognathi lux region / B. A. Illarionov [et al.] // Nucleic Acids Research. - 1988. - Vol. 16, Is. 20. - P9855, DOI 10.1093/nar/16.20.9855 . - ISSN 0305-1048
Кл.слова (ненормированные):
bacterial protein -- luciferase -- article -- bacterial gene -- genetics -- molecular genetics -- nucleotide sequence -- Photobacterium -- Bacterial Proteins -- Base Sequence -- Genes, Bacterial -- Luciferase -- Molecular Sequence Data -- Photobacterium

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, Russian Federation
Institute of Biophysics, Krasnoyarsk, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, 630090, Novosibirsk, Lavrentjev prospect 8, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarionov, B.A.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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9.


   
    Luminescence of Ca(2+)-activated photoprotein obelin initiated by NaOCl and MnCl2. / E. S. Vysotski [et al.] // Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - P301-305 . - ISSN 0884-3996
Кл.слова (ненормированные):
calcium -- chloride -- hypochlorite sodium -- manganese chloride -- manganese derivative -- obelin -- photoprotein -- article -- chemistry -- drug effect -- kinetics -- luminescence -- metabolism -- Calcium -- Chlorides -- Kinetics -- Luminescence -- Luminescent Proteins -- Manganese Compounds -- Sodium Hypochlorite
Аннотация: The luminescence of obelin is initiated by NaOCl in a reaction mixture containing no calcium. The addition of Mn2+ enhances the light emission > 300-fold. Sodium azide and histidine, as singlet oxygen quenchers, inhibit NaOCl-activated obelin luminescence in the presence or absence of Mn2+. This suggests that the addition of NaOCl to the mixture causes singlet oxygen formation (stimulated by Mn2+ ions), and singlet oxygen initiates the light-emitting reaction.

Scopus
Держатели документа:
Laboratory of Photobiology, Russian Academy of Sciences, Krasnoyarsk. : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Vysotski, E.S.; Trofimov, K.P.; Bondar', V.S.; Gitelson, J.I.

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10.


   
    Isolation of bioluminescent functions from Photobacterium leiognathi: analysis of luxA, luxB, luxG and neighboring genes / B. A. Illarrionov [et al.] // Gene. - 1990. - Vol. 86, Is. 1. - P89-94 . - ISSN 0378-1119
Кл.слова (ненормированные):
Bioluminescence -- expression in E. coli -- luciferase -- molecular evolution -- nucleotide sequence -- protein alignment -- recombinant DNA -- luciferase -- amino acid sequence -- article -- bioluminescence -- fungus -- gene structure -- genetic engineering -- heredity -- nonhuman -- nucleotide sequence -- priority journal -- vibrionaceae -- Acyltransferases -- Amino Acid Sequence -- Bacterial Proteins -- Base Sequence -- Cloning, Molecular -- DNA, Bacterial -- Genes, Structural, Bacterial -- Luciferase -- Luminescence -- Molecular Sequence Data -- Operon -- Photobacterium -- Restriction Mapping -- Escherichia coli -- Fungi -- Photobacterium leiognathi -- Vibrio harveyi -- Vibrionaceae
Аннотация: Genes encoding luminescence of Photobacterium leiognathi have been cloned in Escherichia coli. The luminescent clones were readily apparent. Among them, a clone containing a recombinant plasmid with a 13.5-kb insertion was identified. This DNA fragment contained all of the luminescence-encoding genes. The luciferase-encoding genes (lux) in this DNA fragment were localized. We have sequenced a part of the cloned lux region and identified the luxA, luxB and luxG genes encoding the ? and ? subunits of luciferase and a ? protein with an Mr of 26 180, respectively. The analysis of deduced amino acid sequences and comparison with known luciferase sequences from Vibrio harveyi, indicate the common origin of these proteins. В© 1990.

Scopus
Держатели документа:
Krasnoyarsk State University, Krasnoyarsk, 660062, Russian Federation
All-Union Research Institute of Molecular Biology, Novosibirsk Region, 633159, Russian Federation
Institute of Biophysics, Krasnoyarsk, 660036, Russian Federation
Institute of Clinical and Experimental Medicine, Novosibirsk, Russian Federation
Novosibirsk Institute of Bioorganic Chemistry, Novosibirsk, 630090, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Illarrionov, B.A.; Blinov, V.M.; Douchenko, A.P.; Protopopova, M.V.; Karginov, V.A.; Mertvetsov, N.P.; Gitelson, J.I.

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11.


   
    Material balance and diet in bioregenerative life support systems: Connection with coefficient of closure / N. S. Manukovsky [et al.] // Advances in Space Research. - 2005. - Vol. 35, Is. 9 SPEC. ISS. - P1563-1569, DOI 10.1016/j.asr.2005.01.002 . - ISSN 0273-1177
Кл.слова (ненормированные):
Bioregenerative life support system -- Coefficient of closure -- Diet -- Soil-like substrate -- Additives -- Degradation -- Materials balance -- Nitrogen -- Nutrition -- Stoichiometry -- Bioregenerative life support systems -- Coefficient of closure -- Soil-like substrates -- Life support systems (spacecraft) -- vegetable protein -- biomass -- conference paper -- culture medium -- diet -- feces -- growth, development and aging -- human -- methodology -- microclimate -- plant -- urine -- waste management -- Biomass -- Culture Media -- Diet -- Ecological Systems, Closed -- Feces -- Humans -- Life Support Systems -- Plant Proteins -- Plants, Edible -- Urine -- Waste Management
Аннотация: Bioregenerative life support systems (BLSS) with different coefficients of closure are considered. The 66.2% coefficient of closure achieved in "BIOS-3" facility experiments has been taken as a base value. The increase in coefficient of closure up to 72.6-93.0% is planned due to use of soil-like substrate (SLS) and concentrating of urine. Food values were estimated both in a base variant ("BIOS-3"), and with increases in the coefficient of closure. It is shown that food requirements will be more fully satisfied by internal crop production with an increase in the coefficient of closure of the BLSS. Changes of massflow rates on an 'input-output' and inside BLSS are considered. Equations of synthesis and degradation of organic substances in BLSS were examined using a stoichiometric model. The paper shows that at incomplete closure of BLSS containing SLS there is a problem of nitrogen balancing. To compensate for the removal of nitrogen from the system in urine and feces, it is necessary to introduce food and a nitrogen-containing additive. В© 2005 COSPAR. Published by Elsevier Ltd. All rights reserved.

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

Доп.точки доступа:
Manukovsky, N.S.; Kovalev, V.S.; Somova, L.A.; Gurevich, Yu.L.; Sadovsky, M.G.

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12.


   
    Database on natural and transgenic luminous microorganisms: "BIOLUMBASE" / S. E. Medvedeva [и др.] // Mikrobiologiya. - 2005. - Vol. 74, Is. 2. - С. 278-286 . - ISSN 0026-3656
Кл.слова (ненормированные):
Bioluminescence -- Database -- Natural and transgenic luminous microorganisms -- photoprotein -- article -- bacterial gene -- bacterium -- biotechnology -- chemistry -- ecology -- factual database -- genetics -- luminescence -- transgene -- Bacteria -- Biotechnology -- Databases, Factual -- Ecology -- Genes, Bacterial -- Luminescence -- Luminescent Proteins -- Transgenes -- Bacteria (microorganisms)
Аннотация: The database "BiolumBase" is designed for the selection and systematization of available world information on microorganisms containing bioluminescent systems; it includes two sections: "natural" and "transgenic" luminous microorganisms. At present, logic schemes of divisions, classification of the objects, presentation of characteristics, and the inputs of relative information, as well as the necessary program modules including links to the database, are developed. The database is constructed on the basis of published data and our own experimental results; the subsequent linkage of the database to the Internet is envisaged. Users will be able to obtain not only the catalogues of strains but also information concerning the properties and functions of the known species of luminous bacteria, the structure, regulatory mechanisms, and application of bioluminescent systems and genetically engineered constructions with live genes, as well as to find references and to search strains by using any set of attributes. The database will provide information that is of interest for the development of microbial ecology and biotechnology, in particular, for the prediction of biological hazard from the application of transgenic strains.

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:
Medvedeva, S.E.; Boyandin, A.N.; Lankin, Yu.P.; Kotov, D.A.; Kargatova, T.V.; Rodicheva, E.K.; Popova, L.Yu.

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13.


   
    BIOLUMBASE - The database of natural and transgenic bioluminescent organisms / S. E. Medvedeva [et al.] // Luminescence. - 2005. - Vol. 20, Is. 2. - P90-96, DOI 10.1002/bio.809 . - ISSN 1522-7235
Кл.слова (ненормированные):
Bioluminescence -- Database -- Luminous bacteria -- lux gene -- Marine -- article -- bacterial strain -- bacterium culture -- bacterium isolation -- bioluminescence -- data base -- gene construct -- medical information -- transgenics -- wide area network -- Bacteria -- Bacterial Proteins -- Databases, Factual -- Ecology -- Luminescence -- Luminescent Proteins -- Marine Biology -- Organisms, Genetically Modified -- Photobacterium -- Transgenes
Аннотация: The Institute of Biophysics SB RAS hosts and maintains a specialized collection of luminous bacteria (CCIBSO 836) containing over 700 strains isolated in various regions of the world's oceans. The culture collection is a source of lux genes and biologically active substances. The wide application of bioluminescence in medicine and ecology has given importance to analys-ing information on the structure and functioning of bioluminescence systems in natural and transgenic microorganisms, as well as on their features that are closely interrelated with bioluminescence. The aims of our BIOLUMBASE database are: gathering information on microorganisms with lux genes, their analysis and free access, and distribution of this data throughout the global network. The database includes two sections, natural and transgenic luminous microorganisms, and is updated by our own experimental results, the published literature and internet resources. For the future, a publicly available internet site for BIOLUMBASE is planned. This will list the strains and provide comprehensive information on the properties and functions of luminous bacteria, the mechanisms of regulation of bioluminescence systems, constructs with lux genes, and applications of bioluminescence in microbiology, ecology, medicine and biotechnology. It is noteworthy that this database will also be useful for evaluation of biological hazards of transgenic strains. Users will be able to carry out bibliographic and strain searches starting from any feature of interest. Copyright В© 2005 John Wiley & Sons, Ltd.

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

Доп.точки доступа:
Medvedeva, S.E.; Boyandin, A.; Lankin, Y.; Kotov, D.; Rodicheva, E.; Popova, L.

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14.


   
    Immunoelectronmicroscopic study of the nucleoid structure of hydrogen bacteria. / O. A. Mogilnaya [et al.] // Journal of Basic Microbiology. - 1992. - Vol. 32, Is. 6. - P381-387 . - ISSN 0233-111X
Кл.слова (ненормированные):
bacterial DNA -- Alcaligenes -- article -- cell division -- cell nucleus -- Escherichia coli -- immunoelectron microscopy -- ultrastructure -- Alcaligenes -- Cell Division -- Cell Nucleus -- DNA, Bacterial -- Escherichia coli -- Microscopy, Immunoelectron
Аннотация: Electron microscopical studies of the nucleoid structure of hydrogen bacteria using ultrahin sections and spread DNA from bacterial cell lysates revealed a different DNA packaging in the cell. A compact state of the major part of DNA at all growth stages and stability of nucleosome-like structures were shown. The use of antibodies to HU protein of E. coli labelled by protein A-colloidal gold demonstrated the immunological relationship between HU protein of E. coli and histone-like proteins of Alcaligenes eutrophus and their possible role in the nucleosome-like DNA packaging in procariotic genome.

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

Доп.точки доступа:
Mogilnaya, O.A.; Kiselyova, E.V.; Medvedeva, S.E.; Puzir, A.P.; Guseynov, O.A.; Kulyba, N.N.; Kozlov, A.V.

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15.


   
    Untangling metabolic and spatial interactions of stress tolerance in plants. 1. Patterns of carbon metabolism within leaves / K. Y. Biel [et al.] // Protoplasma. - 2010. - Vol. 245, Is. 1. - P49-73, DOI 10.1007/s00709-010-0135-7 . - ISSN 0033-183X
Кл.слова (ненормированные):
Carbon metabolism -- Leaf anatomy -- Leaf form and function -- Maximal ecological utility -- Photosynthesis -- Stress tolerance Spinacia oleracea -- aspartate aminotransferase isoenzyme 1 -- bicarbonate -- carbon -- carbon dioxide -- catalase -- chlorophyll -- malate dehydrogenase -- oxygen -- ribulosebisphosphate carboxylase -- vegetable protein -- article -- enzymology -- histology -- light -- metabolism -- oxidation reduction reaction -- photosynthesis -- physiological stress -- physiology -- plant leaf -- spinach -- theoretical model -- Aspartate Aminotransferase, Cytoplasmic -- Bicarbonates -- Carbon -- Carbon Dioxide -- Catalase -- Chlorophyll -- Light -- Malate Dehydrogenase -- Models, Theoretical -- Oxidation-Reduction -- Oxygen -- Photosynthesis -- Plant Leaves -- Plant Proteins -- Ribulose-Bisphosphate Carboxylase -- Spinacia oleracea -- Stress, Physiological -- Spinacia oleracea
Аннотация: The localization of the key photoreductive and oxidative processes and some stress-protective reactions within leaves of mesophytic C3 plants were investigated. The role of light in determining the profile of Rubisco, glutamate oxaloacetate transaminase, catalase, fumarase, and cytochrome-c-oxidase across spinach leaves was examined by exposing leaves to illumination on either the adaxial or abaxial leaf surfaces. Oxygen evolution in fresh paradermal leaf sections and CO2 gas exchange in whole leaves under adaxial or abaxial illumination was also examined. The results showed that the palisade mesophyll is responsible for the midday depression of photosynthesis in spinach leaves. The photosynthetic apparatus was more sensitive to the light environment than the respiratory apparatus. Additionally, examination of the paradermal leaf sections by optical microscopy allowed us to describe two new types of parenchyma in spinach-pirum mesophyll and pillow spongy mesophyll. A hypothesis that oxaloacetate may protect the upper leaf tissue from the destructive influence of active oxygen is presented. The application of mathematical modeling shows that the pattern of enzymatic distribution across leaves abides by the principle of maximal ecological utility. Light regulation of carbon metabolism across leaves is discussed. В© 2010 Springer-Verlag.

Scopus
Держатели документа:
Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region 142290, Russian Federation
Biosphere Systems International Foundation, Oro Valley, AZ 85755, United States
International Scientific Centre for Organism Extreme States Research, Krasnoyarsk Scientific Centre, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Forest, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk 660036, Russian Federation
Biocompatible Plant Research Institute, College of Natural Sciences, California State University, Chico, CA 95929-0555, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Biel, K.Y.; Fomina, I.R.; Nazarova, G.N.; Soukhovolsky, V.G.; Khlebopros, R.G.; Nishio, J.N.

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16.


   
    Fluorescence of calcium-discharged obelin: The structure and molecular mechanism of emitter formation / F. N. Tomilin [et al.] // Doklady Biochemistry and Biophysics. - 2008. - Vol. 422, Is. 1. - P279-284, DOI 10.1134/S1607672908050086 . - ISSN 1607-6729
Кл.слова (ненормированные):
calcium -- obelin -- photoprotein -- article -- chemical model -- chemical structure -- chemistry -- computer simulation -- light -- protein binding -- protein conformation -- radiation exposure -- Calcium -- Computer Simulation -- Light -- Luminescent Proteins -- Models, Chemical -- Models, Molecular -- Protein Binding -- Protein Conformation

Scopus
Держатели документа:
Kirensky Institute of Physics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 660036, Russian Federation
Siberian Federal University, Krasnoyarsk 660062, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Tomilin, F.N.; Antipina, L.Yu.; Vysotski, E.S.; Ovchinnikov, S.G.; Gitelzon, I.I.

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17.


   
    Affine magnetic sorbents supported on coal ash microspheres for recombinant protein isolation / L. A. Frank [et al.] // Applied Biochemistry and Microbiology. - 2009. - Vol. 45, Is. 2. - P215-220, DOI 10.1134/S0003683809020173 . - ISSN 0003-6838
Кл.слова (ненормированные):
Clytia gregaria -- Obelia longissima
Аннотация: The results of the development and utilization of an affine magnetic sorbent with Ni2+ ions immobilized on coal ash microspheres are reported. The applicability of the material in the isolation of Histag proteins is demonstrated by examples of the recombinant green fluorescent protein from Clytia gregaria and the Ca2+ regulated photoprotein obelin from Obelia longissima. The specific sorption capacity of the sorbent was 2-7 mg/cm3 for medium-size proteins (20-30 kDa). The particles are suitable for chromatography with the presence of chaotropic agents and EDTA. They are easy to manipulate as isolation of a target protein takes 30-35 min. On the one hand, the elevated affinity of the sorbent to proteins rich in native histidines may result in a high degree of irreversible sorption; on the other hand, it allows isolation of such proteins without the introduction of artificial polyhistidine fragments. В© 2009 Pleiades Publishing, Ltd.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660036, Russian Federation
Institute of Chemistry and Chemical Technology, Siberian Branch, Russian Academy of Sciences, Krasnoyarsk, 660049, Russian Federation
Siberian Federal University, Krasnoyarsk, 660041, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Frank, L.A.; Borisova, V.V.; Vereshchagina, T.A.; Fomenko, E.V.; Anshits, A.G.; Gitelson, I.I.

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18.


   
    A QUANTUM CHEMICAL STUDY OF THE FORMATION OF 2-HYDROPEROXY-COELENTERAZINE IN THE Ca2+-REGULATED PHOTOPROTEIN OBELIN [Text] / L. Y. Antipina [et al.] // J. Struct. Chem. - 2011. - Vol. 52, Is. 5. - P870-875. - Cited References: 19. - The work was supported by RFBR (07-04-00930-a), the "Molecular and Cell Biology" Program of the Presidium of the Russian Academy of Sciences, and the Program of the Siberian Division of the Russian Academy of Sciences (project No. 2) within the implementation of the Federal Targeted Program "Scientific and Scientific Pedagogical Personnel of Innovative Russia, 2010" (P333 and P213). . - ISSN 0022-4766
РУБ Chemistry, Inorganic & Nuclear + Chemistry, Physical
Рубрики:
CALCIUM-DISCHARGED OBELIN
   SEMIEMPIRICAL METHODS

   1.7 ANGSTROM

   OPTIMIZATION

   PARAMETERS

   MECHANISM

   FLUORESCENCE

   ELEMENTS

   PROTEIN

   EMITTER

Кл.слова (ненормированные):
coelenterazine -- 2-hydroperoxy-coelenterazine -- Obelia longissima -- Renilla muelleri
Аннотация: The Ca2+-regulated photoprotein obelin determines the luminescence of the marine hydroid Obelia longissima. Bioluminescence is initiated by calcium and appears as a result of the oxidative decarboxylation related to the coelenterazine substrate. The luciferase of the luminescent marine coral Renilla muelleri (RM) also uses coelenterazine as a substrate. However, three proteins are involved in the in vivo bioluminescence of these animals: luciferase, green fluorescent protein, and Ca2+-regulated coelenterazine-binding protein (CBP). In fact, CBP that contains one strongly bound coelenterazine molecule is the RM luciferase substrate in the in vivo bioluminescent reaction. Coelenterazine becomes available for oxygen and the reaction with luciferase only after binding CBP with calcium ions. Unlike Ca2+-regulated photoproteins, the coelenterazine molecule is not activated by oxygen in the CBP molecule. In this work, by means of quantum chemical methods the behavior of substrates in these proteins is analyzed. It is shown that coelenterazine can form different tautomers: CLZ(2H) and CLZ(7H). The formation of 2-hydroperoxy-coelenterazine is studied. According to the obtained data, these proteins use different forms of the substrates for the reaction. In obelin, the substrate is in the CLZ(2H) form that affords hydrogen peroxide. In RM, coelenterazine is in the CLZ(7H) form, and therefore, CBP is not activated by oxygen.

Держатели документа:
[Antipina, L. Yu
Tomilin, F. N.
Ovchinnikov, S. G.] Russian Acad Sci, LV Kirensky Phys Inst, Siberian Div, Krasnoyarsk, Russia
[Vysotskii, E. S.] Russian Acad Sci, Inst Biophys, Siberian Div, Krasnoyarsk, Russia
[Antipina, L. Yu
Ovchinnikov, S. G.] MF Reshetnev Siberian State Aerosp Univ, Krasnoyarsk, Russia
ИФ СО РАН
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Antipina, L.Y.; Tomilin, F.N.; Vysotskii, E.S.; Ovchinnikov, S.G.

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19.


   
    Ligand binding and conformational states of the photoprotein obelin / E. V. Eremeeva [et al.] // FEBS Lett. - 2012. - Vol. 586, Is. 23. - P4173-4179, DOI 10.1016/j.febslet.2012.10.015. - Cited References: 24. - The work was supported by RFBR grant 12-04-00131, by the Program of the Government of Russian Federation "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.058), by the Program "Molecular and Cellular Biology" of RAS. The Wageningen University Sandwich PhD-Fellowship Program supported E.V.E. . - ISSN 0014-5793
РУБ Biochemistry & Molecular Biology + Biophysics + Cell Biology
Рубрики:
RECOMBINANT OBELIN
   CRYSTAL-STRUCTURE

   LIGHT-EMISSION

   APO-AEQUORIN

   BIOLUMINESCENCE

   COELENTERAZINE

   LUMINESCENCE

   STABILITY

   ANGSTROM

   PROTEINS

Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Photoprotein -- Thermostability
Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformational states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

Держатели документа:
[Eremeeva, Elena V.
Westphal, Adrie H.
van Mierlo, Carlo P. M.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Eremeeva, Elena V.
Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Vysotski, Eugene S.] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Vysotski, E.S.; Westphal, A.H.; van Mierlo, CPM; van Berkel, WJH

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20.


   
    Bioluminescent re-engineered proteins as effective reporters for in vitro assay / L. A. Frank [et al.] // Luminescence. - 2012. - Vol. 27, Is. 2. - P116-116. - Cited References: 2 . - ISSN 1522-7235
РУБ Biochemistry & Molecular Biology


Держатели документа:
[Frank, L. A.
Krasitskaya, V. V.
Kudryavtsev, A. N.
Burakova, L. P.
Stepanyuk, G. A.
Markova, S. V.
Vysotski, E. S.] Inst Biophys SB RAS, Photobiol Lab, Krasnoyarsk 660036, Russia
[Frank, L. A.
Kudryavtsev, A. N.
Burakova, L. P.] Siberian Fed Univ, Krasnoyarsk 660041, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Frank, L.A.; Krasitskaya, V.V.; Kudryavtsev, A.N.; Burakova, L.P.; Stepanyuk, G.A.; Markova, S.V.; Vysotski, E.S.

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