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Content of metals in compartments of ecosystem of a Siberian pond / M. I. Gladyshev [et al.] // Archives of Environmental Contamination and Toxicology. - 2001. - Vol. 41, Is. 2. - P157-162, DOI 10.1007/s002440010233 . - ISSN 0090-4341
Кл.слова (ненормированные):
aluminum -- cadmium -- calcium -- chromium -- copper -- heavy metal -- iron -- lead -- magnesium -- manganese -- nickel -- potassium -- sodium -- zinc -- aquatic ecosystem -- biological uptake -- heavy metal -- pond -- article -- bioaccumulation -- ecosystem -- fish -- nonhuman -- pond -- priority journal -- Russian Federation -- sediment -- soil pollution -- water contamination -- Animals -- Ecosystem -- Environmental Monitoring -- Fishes -- Geologic Sediments -- Invertebrates -- Metals, Heavy -- Plants -- Water Pollutants -- Russian Federation
Аннотация: During three field seasons (June-September) of 1997-99 contents of Na, K, Ca, Mg, Fe, Mn, Zn, Cu, Al, Cr, Ni, Cd, and Pb were determined in compartments of ecosystem (surrounding soils, bottom sediments, water, zoobenthos, macrophytes, and fish) of a fish and recreation pond situated at the edge of Krasnoyarsk City (Siberia, Russia). Contents of most parts of metals in soils, water, and macrophytes significantly correlated with each other. As concluded, their contents were determined by natural, general, geochemical peculiarities of the region. Heavy metals, contents of which were higher than federal upper limits of concentration, were revealed. In muscles of fish with different feeding spectra - crucian and perch - concentrations of some metals differed significantly; correlation graphs for metals also had different structures. Comparison of our data with those on diverse aquatic ecosystems of Siberia, Europe, North America, and China published in the last decade was carried out. It was concluded that a distribution of heavy metals in the compartments of an aquatic ecosystem presently have to be determined for each particular water body until general regularities are discovered.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch of Russian Academy of Sciences, Akademgorodok, Krasnoyarsk, 660036, Russian Federation
Krasnoyarsk State Agricultural University, Mira av., 88, Krasnoyarsk, 660049, Russian Federation
Krasnoyarsk State University, Svobodny av., 79, Krasnoyarsk, 660042, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Gladyshev, M.I.; Gribovskaya, I.V.; Moskvicheva, A.V.; Muchkina, E.Y.; Chuprov, S.M.; Ivanova, E.A.

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Influence of high concentrations of mineral salts on production process and NaCl accumulation by Salicornia europaea plants as a constituent of the LSS phototroph link / N. A. Tikhomirova [et al.] // Advances in Space Research. - 2005. - Vol. 35, Is. 9 SPEC. ISS. - P1589-1593, DOI 10.1016/j.asr.2005.01.055 . - ISSN 0273-1177
Кл.слова (ненормированные):
BLSS -- Intensity of PAR -- Mineral nutrition -- Productivity -- Salicornia europaea -- Biomass -- Concentration (process) -- Nitrogen -- Nutrition -- Photosynthesis -- Productivity -- Sodium chloride -- Bioregenerative life support systems (BLSS) -- Intensity of PAR -- Mineral nutrition -- Salicornia europaea -- Plants (botany) -- calcium -- magnesium -- nitrogen -- phosphorus -- potassium -- sodium chloride -- sulfur -- urea -- biomass -- conference paper -- culture medium -- dose response -- drug effect -- goosefoot -- growth, development and aging -- human -- light -- metabolism -- microclimate -- radiation exposure -- urine -- Biomass -- Calcium -- Chenopodiaceae -- Culture Media -- Dose-Response Relationship, Drug -- Ecological Systems, Closed -- Humans -- Life Support Systems -- Light -- Magnesium -- Nitrogen -- Phosphorus -- Potassium -- Sodium Chloride -- Sulfur -- Urea -- Urine
Аннотация: Use of halophytes (salt-tolerant vegetation), in a particular vegetable Salicornia europaea plants which are capable of utilizing NaCl in rather high concentrations, is one of possible means of NaCl incorporation into mass exchange of bioregenerative life support systems. In preliminary experiments it was shown that S. europaea plants, basically, could grow on urine pretreated with physicochemical processing and urease-enzyme decomposing of urea with the subsequent ammonia distillation. But at the same time inhibition of the growth process of the plants was observed. The purpose of the given work was to find out the influence of excessive quantities of some mineral elements contained in products of physicochemical processing of urine on the production process and NaCl accumulation by S. europaea plants. As the content of mineral salts in the human liquid wastes (urine) changed within certain limits, two variants of experimental solutions were examined. In the first variant, the concentration of mineral salts was equivalent to the minimum salt content in the urine and was: K - 1.5 g/l, P - 0.5 g/l, S - 0.5 g/l, Mg - 0.07 g/l, Ca - 0.2 g/l. In the second experimental variant, the content of mineral salts corresponded to the maximum salt content in urine and was the following: K - 3.0 g/l, P - 0.7 g/l, S - 1.2 g/l, Mg - 0.2 g/l, Ca - 0.97 g/l. As the control, the Tokarev nutrient solution containing nitrogen in the form of a urea, and the Knop nutrient solution with nitrogen in the nitrate form were used. N quantity in all four variants made up 177 mg/l. Air temperature was 24 В°C, illumination was continuous. Light intensity was 690 ?mol/m2s of photosynthetically active radiation. NaCl concentration in solutions was 1%. Our researches showed that the dry aboveground biomass of an average plant of the first variant practically did not differ from the control and totaled 11 g. In the second variant, S. europaea productivity decreased and the dry aboveground biomass of an average plant totaled 8 g. The increase of K quantity in the experimental solutions resulted in an elevated content of the element in the plants. The increase of K uptake in the second experimental variant was accompanied by a 30-50% decrease of Na content in comparison with the other variants. Comparative Na content in the other variants was practically identical. N, Mg and P content in the control and experimental variants was also practically identical. The increase of S quantity in the second experimental variant also increased S uptake by the plants. But Ca quantity, accumulated in aboveground plants biomass in the experimental variants was lower than in the control. NaCl uptake by plants, depending on the concentration of mineral salts in the experimental solutions, ranged from 8 g (maximum salt content) up to 15 g (minimum salt content) on a plant growth area that totaled 0.032 m2. Thus, high concentrations of mineral salts simulating the content of mineral salts contained in urine did not result in a significant decrease of S. europaea productivity. The present work also considers the influence of higher light intensity concentrations on productivity and NaCl accumulation by S. europaea plants grown on experimental solutions with high salt content. В© 2005 COSPAR. Published by Elsevier Ltd. All rights reserved.

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

Доп.точки доступа:
Tikhomirova, N.A.; Ushakova, S.A.; Kovaleva, N.P.; Gribovskaya, I.V.; Tikhomirov, A.A.

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Effect of NaCl concentration on productivity and mineral composition of Salicornia europaea as a potential crop for utilization NaCl in LSS / S. A. Ushakova [et al.] // Advances in Space Research. - 2005. - Vol. 36, Is. 7. - P1349-1353, DOI 10.1016/j.asr.2004.09.017 . - ISSN 0273-1177
Кл.слова (ненормированные):
Life support system -- NaCl -- Salicornia europaea -- Space biology -- Calcium -- Concentration (process) -- Minerals -- Photosynthesis -- Plants (botany) -- Salinity measurement -- Sodium chloride -- Vegetation -- Life support systems -- Liquid wastes -- NaCl -- Salicornea europea -- Space biology -- Space research
Аннотация: The accumulation of solid and liquid wastes in manmade ecosystems presents a problem that has not been efficiently solved yet. Urine, containing NaCl, are part of these products. This is an obstacle to the creation of biological systems with a largely closed material cycling, because the amount of solid and liquid wastes in them must be reduced to a minimum. A possible solution to the problem is to select plant species capable of utilizing sufficiently high concentrations of NaCl, edible for humans, and featuring high productivity. Until recently, the life support systems have included the higher plants that were either sensitive to salinization (wheat, many of the legumes, carrot, potato, maize) or relatively salt-resistant (barley, sugar beet, spinach). Salicomia europaea, whose above-ground part is fully edible for humans, is one of the most promising candidates to be included in life support systems. It is reported in the literature that this plant is capable of accumulating up to 50% NaCl (dry basis). Besides, excessive accumulation of sodium ions should bring forth a decrease in the uptake of potassium ions and other biogenic elements. The aim of this work is to study the feasibility of using S. europaea plants in growth chambers to involve NaCl into material cycling. Plants were grown in vegetation chambers at the irradiance of 100 or 150 W/m2 PAR (photosynthetically active radiation) and the air temperature 24 В°C, by two methods. The first method was to grow the plants on substrate - peat. The peat was supplemented with either 3% NaCl (Variant 1) or 6% NaCl (Variant 2) of the oven-dry mass of the peat. The second method was to grow the plants in water culture, using the solution with a full complement of nutrients, which contained 0.0005% of NaCl, 1% or 2%. The study showed that the addition of NaCl to the substrate or to the solution resulted in the formation of more succulent plants, which considerably increased their biomass. The amount of NaCl uptake was the highest in the plants grown in water culture, 2.6 g per plant. As the sodium uptake increased, the consumption of potassium and the sum of the reduced N forms decreased twofold. The uptake of calcium and magnesium by plants decreased as the NaCl concentration increased; the smallest amounts were taken up by S. europaea grown in water culture. Salinity had practically no effect on the uptake of phosphorus and sulfur. Thus, S. europaea is a promising candidate to be included in life support systems; of special interest is further research on growing these plants in water culture. В© 2005 COSPAR. Published by Elsevier Ltd. All rights reserved.

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

Доп.точки доступа:
Ushakova, S.A.; Kovaleva, N.P.; Gribovskaya, I.V.; Dolgushev, V.A.; Tikhomirova, N.A.

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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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^a343.17.27.07.09.05^2VINITI
C36

Ca{2+}-активируемый фотопротеин обелин как индикатор кальциевого транспорта в протеолипосомах, включающих мембраны Т-системы скелетных мышц [Текст] : научное издание / В. С. Бондарь [и др.] // Биохимия. - 1991. - Т. 56, N 5. - С. 806-811 . - ISSN 0320-9725

ГРНТИ

34.17.27

РУБ 343.17.27.07.09.05
Рубрики:
ФОТОПРОТЕИНЫ
   КАЛЬЦИЙ-АКТИВИРУЕМЫЕ
   ОБЕЛИН
   ТРАНСПОРТ КАЛЬЦИЯ
   ПРОТЕОЛИПОСОМЫ
   МЕМБРАНЫ Т-СИСТЕМЫ СКЕЛЕТНЫХ МЫШЦ
   PHOTOPROTEIN
   CALCIUM TRANSPORT
   OBELIN
   PROTEOLIPOSOME
   MEMBRANE
Аннотация: В работе представлены данные о Ca{2+}-активируемом фотопротеине обелине как индикаторе кальциевого транспорта в протеолипосомах. Показано, что протеолипосомы, сформированные из лецитина и мембран T-системы скелетных мышц кролика, обладают проницаемостью к ионам кальция, активируемой 10{-5 }M BAY K-8644; 5*10{-5 }M нитендипин ингибирует действие BAY K-8644. Липосомы не проявляли чувствительности к исследуемым агентам. Ca{2+}-активируемый фотопротеин обелин является перспективным инструментом для изучения быстрых кальциевых потоков
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Бондарь, В.С.; Высоцкий, Е.С.; Рожманова, О.М.; Воронина, С.Г.

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Cultivation of multipotent mesenchymal bone marrow cells on matrixes made of resorbable bioplastotan / E. I. Shishatskaya [и др.] // Cellular Transplantation and Tissue Engineering. - 2013. - Vol. 8, Is. 1. - С. 57-65 . - ISSN 1815-445X
Кл.слова (ненормированные):
Alkaline phosphatase -- Differentiation -- Extracellular calcium precipitates -- Multipotent mesenchymal stromal cells -- Osteopontin -- Resorbable bioplastotan
Аннотация: Series of cell carriers made of resorbable polyester Bioplastotan, which is a copolymer of 3- And 4-hydroxybutyric acid, are characterized in this work. With use of various technologies membranes, 3D scaffolds, and nanomatrixes formed by ultrafine fibers produced with electrostatic spinning were constructed. All types of scaffolds provide adhesion of multipotent mesenchymal stromal cells and are suitable for the cultivation and differentiation of cells in the osteoblastes, that confirmed by detection of extracellular calcium precipitates, alkaline phosphatase activity and osteopontin production in cell culture. В© Human stem cells institute, 2013.

Scopus
Держатели документа:
Siberian Branch, Institute of Biophisycs, RAS, Krasnoyarsk, Russian Federation
Siberian Federal University, Krasnoyarsk, Russian Federation
Siberian Branch, L.V. Kirensky Institute of Physics, RAS, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Shishatskaya, E.I.; Nikolaeva, E.D.; Shumilova, A.A.; Shabanov, A.V.; Volova, T.G.

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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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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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Removal of essential ligand in N-terminal calcium binding domain of obelin does not inactivate the photoprotein or reduce its calcium sensitivity, but dramatically alters the kinetics of the luminescent reaction [Text] / V. A. Illarionova [et al.] ; ed.: JW Hastings, LJ Kricka, J Kricka, // BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS : JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - P431-434. - Cited References: 0 . - 4. - ISBN 0-471-97502-8

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical

: 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Illarionova, V.A.; Illarionov, B.A.; Bondar, V.S.; Vysotski, E.S.; Blinks, J.R.; Hastings, JW \ed.\; Kricka, LJ \ed.\; Kricka,, J \ed.\

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10.

SEQUENCE OF THE CDNA-ENCODING THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA [Text] / B. A. ILLARIONOV [et al.] // Gene. - 1995. - Vol. 153, Is. 2. - P273-274, DOI 10.1016/0378-1119(94)00797-V. - Cited References: 6 . - 2. - ISSN 0378-1119

РУБ Genetics & Heredity
Рубрики:
CA-2+-ACTIVATED PHOTOPROTEIN
AEQUORIN
CLONING
Кл.слова (ненормированные):
BIOLUMINESCENCE -- CALCIUM -- GENE -- PLASMID -- MARINE COELENTERATES
Аннотация: A cDNA clone encoding the Ca2+-activated photoprotein, obelin (Obl), from Obelia longissima was sequenced. The nucleotide (nt) sequence contained two long overlapping open reading frames (ORFs), one of which encoded apoobelin (apoObl). The deduced amino acid (aa) sequence of apoObl revealed that this 195-aa protein has three EF-hand structures that are characteristic for Ca2+-binding domains. Strong aa homology was shown among apoObl, apoaequorin and apoclytin. The second ORF present in the obl cDNA consists of 139 codons and encodes a very basic protein with a calculated pI of 10.56 and a molecular mass of 16153 Da.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
ILLARIONOV, B.A.; BONDAR, V.S.; ILLARIONOVA, V.A.; VYSOTSKI, E.S.

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11.

MN2+-ACTIVATED LUMINESCENCE OF THE PHOTOPROTEIN OBELIN [Text] / E. S. VYSOTSKI [et al.] // Arch. Biochem. Biophys. - 1995. - Vol. 316, Is. 1. - P92-99, DOI 10.1006/abbi.1995.1014. - Cited References: 38 . - 8. - ISSN 0003-9861

РУБ Biochemistry & Molecular Biology + Biophysics
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   CA-2+-ACTIVATED PHOTOPROTEIN
   MESSENGER-RNA
   BEROE-OVATA
   AEQUORIN
   PURIFICATION
   PROTEIN
   CDNA
   EXTRACTION
Аннотация: The light emission of obelin may be initiated by Mn2+ under alkaline conditions. The luminescence takes place in a pH range from 7 to 12 with a sharp optimum at 11.75. The first-order rate constant for Mn2+-activated luminescence decay is more than 9 s(-1), while that for Ca2+-activated luminescence decay is only 6.9 s(-1). The Mn2+ concentration-effect curve for obelin determined with simple dilutions of manganese salt is a sigmoid curve, The slope of the curve is moderately dependent on the pH and was not more than 1 within the pH range tested. The maximal light emission, which is initiated by 3.6 X 10(-5) M Mn2+ at pH 11.75 was about 10% of the maximal Ca2+-activated luminescence. Mg2+ ions inhibit the Mn2+-activated luminescence of obelin. The addition of OH. and O-2(-) scavengers did not influence the Mn2+-activated luminescence, but when singlet oxygen quenchers were added, the Mn2+-dependent light emission was inhibited. This suggests that the O-1(2) might be formed and itself be responsible for chromophore oxidation attended with light emission. NEM and Na2S2O4 inhibit the Mn2+-initiated light emission of obelin completely, showing that endogenous hydroperoxide and SH-group(s) of the photoprotein are essential for both Ca2+-activated and Mn2+-activated light emission of obelin. (C) 1995 Academic Press, Inc.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
VYSOTSKI, E.S.; TROFIMOV, C.P.; BONDAR, V.S.; FRANK, L.A.; MARKOVA, S.V.; ILLARIONOV, B.A.

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12.

THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN AS AN INDICATOR OF CALCIUM-TRANSPORT IN PROTEOLIPOSOMES CONTAINING MEMBRANES OF THE T-SYSTEM OF SKELETAL-MUSCLES [Text] / V. S. BONDAR [et al.] // Biochem.-Moscow. - 1991. - Vol. 56, Is. 5. - P546-550. - Cited References: 12 . - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CHANNEL
   CA-2+
   MODULATION
   BINDING
Кл.слова (ненормированные):
CA2+-TRANSPORT -- CA2+-ACTIVATED PHOTOPROTEIN OBELIN -- T-SYSTEM -- 1,4-DIHYDROPYRIDINES -- LIPOSOMES
Аннотация: Data are presented on the Ca2+-activated photoprotein obelin as an indicator of calcium transport in proteoliposomes. Proteoliposomes formed from lecithin and membranes of the T-system of rabbit skeletal muscles were found to exhibit permeability to calcium ions activated by 10(-5) M BAU K-8644; 5.10(-5) M nitrendipine inhibits the action of BAU K-8644. Liposomes did not exhibit sensitivity to the investigated agents. The Ca2+-activated photoprotein obelin is a promising tool for studying fast calcium currents.

Держатели документа:
ACAD SCI USSR,INST BIOPHYS,KRASNOYARSK,USSR
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
BONDAR, V.S.; VYSOTSKII, E.S.; ROZHMANOVA, O.M.; VORONINA, S.G.

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13.

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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14.

Oxygen Activation of Apo-obelin-Coelenterazine Complex / E. V. Eremeeva [et al.] // ChemBioChem. - 2013. - Vol. 14, Is. 6. - P739-745, DOI 10.1002/cbic.201300002. - Cited References: 46. - The work was supported by grants from the RFBR 12-04-91153, and NSFC 31270795 and 31021062, by the Russian Federation Government Program "Measures to Attract Leading Scientists to Russian Educational Institutions" (grant 11.G34.31.0058), "Molecular and Cellular Biology" of RAS, President of the Russian Federation "Leading Science School" (grant 1044.2012.2). E.V.E. was supported by a Wageningen University Sandwich PhD Fellowship Program. . - ISSN 1439-4227

РУБ Biochemistry & Molecular Biology + Chemistry, Medicinal
Рубрики:
GREEN-FLUORESCENT PROTEIN
   JELLYFISH CLYTIA-GREGARIA
   CRYSTAL-STRUCTURE
   CA2+-DISCHARGED PHOTOPROTEIN
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   MOLECULAR-OXYGEN
   AEQUORIN
   CALCIUM
   BIOLUMINESCENCE
Кл.слова (ненормированные):
aequorin -- coelenterazine -- luminescence -- photoprotein -- protein folding
Аннотация: Ca2+-regulated photoproteins use a noncovalently bound 2-hydroperoxycoelenterazine ligand to emit light in response to Ca2+ binding. To better understand the mechanism of formation of active photoprotein from apoprotein, coelenterazine and molecular oxygen, we investigated the spectral properties of the anaerobic apo-obelincoelenterazine complex and the kinetics of its conversion into active photoprotein after exposure to air. Our studies suggest that coelenterazine bound within the anaerobic complex might be a mixture of N7-protonated and C2() anionic forms, and that oxygen shifts the equilibrium in favor of the C2() anion as a result of peroxy anion formation. Proton removal from N7 and further protonation of peroxy anion and the resulting formation of 2-hydroperoxycoelenterazine in obelin might occur with the assistance of His175. It is proposed that this conserved His residue might play a key role both in formation of active photoprotein and in Ca2+-triggering of the bioluminescence reaction.

Держатели документа:
[Eremeeva, Elena V.
Natashin, Pavel V.
Liu, Zhi-Jie] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[Eremeeva, Elena V.
Natashin, Pavel V.
Vysotski, Eugene S.] Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia
[Eremeeva, Elena V.
Natashin, Pavel V.
Vysotski, Eugene S.] Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
[Eremeeva, Elena V.
Natashin, Pavel V.
Vysotski, Eugene S.] Siberian Fed Univ, Chair Biophys, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia
[Eremeeva, Elena V.
van Berkel, Willem J. H.] Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands
[Song, Lei
Zhou, Yuguang] Chinese Acad Sci, China Gen Microbiol Culture Collect Ctr, Inst Microbiol, Beijing 100101, Peoples R China
[Liu, Zhi-Jie] Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Eremeeva, E.V.; Natashin, P.V.; Song, L...; Zhou, Y.G.; van Berkel, WJH; Liu, Z.J.; Vysotski, E.S.

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15.

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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16.

The light-sensitive photoprotein berovin from the bioluminescent ctenophore Beroe abyssicola: a novel type of Ca2+-regulated photoprotein / S. V. Markova [et al.] // FEBS J. - 2012. - Vol. 279, Is. 5. - P856-870, DOI 10.1111/j.1742-4658.2012.08476.x. - Cited References: 63. - The authors thank Natalia Chervyakova from Department of Zoology of Invertebrates of Moscow State University for the photo of the White Sea ctenophore Beroe abyssicola. This work was supported by RFBR grant 09-04-00172, by grant 64987.2010.4, Molecular and Cellular Biology program of RAS, and Bayer Pharma AG (Germany). . - ISSN 1742-464X

РУБ Biochemistry & Molecular Biology
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   C-TERMINAL PROLINE
   SEQUENCE-ANALYSIS
   MNEMIOPSIS-SP
   COELENTERAZINE-BINDING
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   CRYSTAL-STRUCTURES
   EXCITED-STATE
   CDNA CLONING
Кл.слова (ненормированные):
bioluminescence -- calcium -- coelenterazine -- luciferase -- mammalian expression
Аннотация: Light-sensitive Ca2+-regulated photoproteins are responsible for the bright bioluminescence of ctenophores. Using functional screening, four full-size cDNA genes encoding the same 208-amino-acid polypeptide were isolated from two independent cDNA libraries prepared from two Beroe abyssicola specimens. Sequence analysis revealed three canonical EF-hand calcium-binding sites characteristic of Ca2+-regulated photoproteins, but a very low degree of sequence identity (2729%) with aequorin-type photoproteins, despite functional similarities. Recombinant berovin was expressed in Escherichia coli cells, purified, converted to active photoprotein and characterized. Active berovin has absorption maxima at 280 and 437 nm. The Ca2+-discharged protein loses visible absorption, but exhibits a new absorption maximum at 335 nm. The berovin bioluminescence is blue (?max = 491 nm) and a change in pH over the range 6.09.5 has no significant effect on the light emission spectrum. By contrast, the fluorescence of Ca2+-discharged protein (?ex = 350 nm) is pH sensitive: at neutral pH the maximum is at 420 nm and at alkaline pH there are two maxima at 410 and 485 nm. Like native ctenophore photoproteins, recombinant berovin is also inactivated by light. The Ca2+ concentrationeffect curve is a sigmoid with a slope on a loglog plot of similar to 2.5. Although this curve for berovin is very similar to those obtained for obelin and aequorin, there are evident distinctions: berovin responds to calcium changes at lower concentrations than jellyfish photoproteins and its Ca2+-independent luminescence is low. Recombinant berovin was successfully expressed in mammalian cells, thereby demonstrating potential for monitoring intracellular calcium.

Держатели документа:
[Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Markova, Svetlana V.
Burakova, Ludmila P.
Malikova, Natalia P.
Frank, Ludmila A.
Vysotski, Eugene S.] Siberian Fed Univ, Dept Biophys, Krasnoyarsk, Russia
[Golz, Stefan] Bayer Pharma AG, Global Drug Discovery, Wuppertal, Germany
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Markova, S.V.; Burakova, L.P.; Golz, S...; Malikova, N.P.; Frank, L.A.; Vysotski, E.S.

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17.

Coelenterazine-v ligated to Ca2+-triggered coelenterazine-binding protein is a stable and efficient substrate of the red-shifted mutant of Renilla muelleri luciferase [Text] / G. A. Stepanyuk [et al.] // Anal. Bioanal. Chem. - 2010. - Vol. 398, Is. 4. - P1809-1817, DOI 10.1007/s00216-010-4106-9. - Cited References: 39. - This work was supported by grant 09-04-12022 of the Russian Foundation for Basic Research, "Molecular and Cell Biology" program of Russian Academy of Sciences, by the SB RAS grant No. 2, and by the SB RAS Lavrentiev grant for Young Scientists. . - ISSN 1618-2642

РУБ Biochemical Research Methods + Chemistry, Analytical
Рубрики:
GREEN-FLUORESCENT PROTEIN
   BIOLUMINESCENT REPORTER
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   RECOMBINANT OBELIN
   GENE-EXPRESSION
   IN-VIVO
   CDNA
   CLONING
   PURIFICATION
Кл.слова (ненормированные):
Bioluminescence -- Coelenterazine -- Calcium -- Imaging
Аннотация: It has been shown that the coelenterazine analog, coelenterazine-v, is an efficient substrate for a reaction catalyzed by Renilla luciferase. The resulting bioluminescence emission maximum is shifted to a longer wavelength up to 40 nm, which allows the use of some "yellow" Renilla luciferase mutants for in vivo imaging. However, the utility of coelenterazine-v in small-animal imaging has been hampered by its instability in solution and in biological tissues. To overcome this drawback, we ligated coelenterazine-v to Ca2+-triggered coelenterazine-binding protein from Renilla muelleri, which apparently functions in the organism for stabilizing and protecting coelenterazine from oxidation. The coelenterazine-v bound within coelenterazine-binding protein has revealed a greater long-term stability at both 4 and 37 degrees C. In addition, the coelenterazine-binding protein ligated by coelenterazine-v yields twice the total light over free coelenterazine-v as a substrate for the red-shifted R. muelleri luciferase. These findings suggest the possibility for effective application of coelenterazine-v in various in vitro assays.

Держатели документа:
[Stepanyuk, Galina A.
Malikova, Natalia P.
Markova, Svetlana V.
Vysotski, Eugene S.] Russian Acad Sci, Inst Biophys, Siberian Branch, Photobiol Lab, Krasnoyarsk 660036, Russia
[Unch, James] Promega Biosci LLC, San Luis Obispo, CA 93401 USA
[Lee, John] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Unch, J...; Malikova, N.P.; Markova, S.V.; Lee, J...; Vysotski, E.S.

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18.

Crystal structure of coelenterazine-binding protein from Renilla muelleri at 1.7 angstrom: Why it is not a calcium-regulated photoprotein [Text] / G. A. Stepanyuk [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 4. - P442-447, DOI 10.1039/b716535h. - Cited References: 49 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
HYDROID OBELIA-GENICULATA
   AMINO-ACID-SEQUENCE
   CA2+-REGULATED PHOTOPROTEINS
   RENIFORMIS LUCIFERASE
   ENERGY-TRANSFER
   CDNA CLONING
   BIOLUMINESCENCE
   AEQUORIN
   PURIFICATION
   EXPRESSION
Аннотация: Bioluminescence in the sea pansy Renilla involves two distinct proteins, a Ca2+-triggered coelenterazine-binding protein (CBP), and Renilla luciferase. CBP contains one tightly bound coelenterazine molecule, which becomes available for reaction with luciferase and O-2 only subsequent to Ca2+ binding. CBP belongs to the EF-hand superfamily of Ca2+-binding proteins and contains three "EF-hand" Ca2+-binding sites. The overall spatial structure of recombinant selenomethionine-labeled CBP determined at 1.7 angstrom, is found to approximate the protein scaffold characteristic of the class of Ca2+-regulated photoproteins. Photoproteins however, catalyze molecular oxygen addition to coelenterazine producing a 2-hydroperoxycoelenterazine intermediate, which is stabilized within the binding cavity in the absence of Ca2+. Addition of Ca2+ triggers the bioluminescence reaction. However in CBP this first step of oxygen addition is not allowed. The different amino acid environments and hydrogen bond interactions within the binding cavity are proposed to account for the different properties of the two classes of proteins.

Держатели документа:
[Liu, Zhi-Jie] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[Stepanyuk, Galina A.
Lee, John
Vysotski, Eugene S.
Wang, Bi-Cheng] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
[Stepanyuk, Galina A.
Markova, Svetlana S.
Frank, Ludmila A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Photobiol Lab, Inst Biophys, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Stepanyuk, G.A.; Liu, Z.J.; Markova, S.S.; Frank, L.A.; Lee, J...; Vysotski, E.S.; Wang, B.C.

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19.

Obelin mutants with altered affinity to calcium and bioluminescence colour [Text] / N. P. Malikova, E. S. Vysotski // Luminescence. - 2008. - Vol. 23, Is. 2. - P84-84. - Cited References: 0 . - ISSN 1522-7235

РУБ Biochemistry & Molecular Biology

Держатели документа:
[Malikova, N. P.
Vysotski, E. S.] Russian Acad Sci, Inst Biophys, Photobiol Lab, Siberian Branch, Krasnoyarsk 660036, Russia
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50
Доп.точки доступа:
Malikova, N.P.; Vysotski, E.S.

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20.

Coelenterazine-binding protein of Renilla muelleri: cDNA cloning, overexpression, and characterization as a substrate of luciferase [Text] / M. S. Titushin [et al.] // Photochem. Photobiol. Sci. - 2008. - Vol. 7, Is. 2. - P189-196, DOI 10.1039/b713109g. - Cited References: 41 . - ISSN 1474-905X

РУБ Biochemistry & Molecular Biology + Biophysics + Chemistry, Physical
Рубрики:
CRYSTAL-STRUCTURE
   LIGHT-EMISSION
   CA2+-REGULATED PHOTOPROTEINS
   BIOLUMINESCENT REPORTER
   RENIFORMIS LUCIFERASE
   ANGSTROM RESOLUTION
   RECOMBINANT OBELIN
   ENERGY-TRANSFER
   EXCITED-STATE
   CALCIUM
Аннотация: The Renilla bioluminescent system in vivo is comprised of three proteins-the luciferase, green-fluorescent protein, and coelenterazine-binding protein (CBP), previously called luciferin-binding protein (LBP). This work reports the cloning of the full-size cDNA encoding CBP from soft coral Renilla muelleri, its overexpression and properties of the recombinant protein. The apo-CBP was quantitatively converted to CBP by simple incubation with coelenterazine. The physicochemical properties of this recombinant CBP are determined to be practically the same as those reported for the CBP (LBP) of R. reniformis. CBP is a member of the four-EF-hand Ca2+-binding superfamily of proteins with only three of the EF-hand loops having the Ca2+-binding consensus sequences. There is weak sequence homology with the Ca2+-regulated photoproteins but only as a result of the necessary Ca2+-binding loop structure. In combination with Renilla luciferase, addition of only one Ca2+ is sufficient to release the coelenterazine as a substrate for the luciferase for bioluminescence. This combination of the two proteins generates bioluminescence with higher reaction efficiency than using free coelenterazine alone as the substrate for luciferase. This increased quantum yield, a difference of bioluminescence spectra, and markedly different kinetics, implicate that a CBP-luciferase complex might be involved.

Держатели документа:
[Titushin, Maxim S.
Markova, Svetlana V.
Frank, Ludmila A.
Malikova, Natalia P.
Stepanyuk, Galina A.
Vysotski, Eugene S.] Russian Acad Sci, Siberian Branch, Inst Biophys, Photobiol Lab, Krasnoyarsk 660036, Russia
[Lee, John
Vysotski, Eugene S.] Univ Georgia, Dept Biochem & Mol Biol, Athens, GA 30602 USA
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Titushin, M.S.; Markova, S.V.; Frank, L.A.; Malikova, N.P.; Stepanyuk, G.A.; Lee, J...; Vysotski, E.S.

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