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Behaviour of the residue of glutamic acid on self-organization of protein molecules / P. I. Belobrov // Biophysics. - 1975. - Vol. 20, Is. 1. - P18-21 . - ISSN 0006-3509
Кл.слова (ненормированные):
glutamic acid -- protein -- computer analysis -- in vitro study -- theoretical study
Аннотация: The method of atom-atom potentials has been used to study the glutamyl dipeptide in ionized (glu-) and non-ionized (glu) states. A calculation has been made with a computer of the conformational maps and the statistical sums of glu and glu-. It was found that on transition of glu > glu- fall in the energy exceeds the free energy of initiation of the helix with an increased probability of the helical state of the molecule of glu-. From this it is concluded that glu- may in certain conditions be the embryo of the helix on self-organization of protein. В© 1975.

Scopus
Держатели документа:
Institute of Physics, the Siberian Division, U.S.S.R. Academy of Sciences, Krasnoyarsk, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Belobrov, P.I.

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Behavior of glutamic acid residue during self arrangement of protein molecules (Russian) / P. I. Belobrov // Biofizika. - 1975. - Vol. 20, Is. 1. - С. 23-25 . - ISSN 0006-3029
Кл.слова (ненормированные):
glutamic acid -- protein -- in vitro study -- theoretical study

Scopus
Держатели документа:
Inst. Phys., Siberian Branch Ac. Sci. USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Belobrov, P.I.

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Biochemical composition of several blue green algae and Chlorella / N. I. Trubachev, I. I. Gitel'zon, G. S. Kalacheva // Applied Biochemistry and Microbiology. - 1977. - Vol. 12, Is. 2. - P155-161 . - ISSN 0003-6838
Кл.слова (ненормированные):
fatty acid -- lipid -- protein -- vitamin -- alga -- blue green alga -- chlorella -- in vitro study -- microorganism -- plant -- theoretical study

Scopus
Держатели документа:
Inst. Phys., Siberian Branch, Acad. Scis USSR, Krasnoyarsk, Russia : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Trubachev, N.I.; Gitel'zon, I.I.; Kalacheva, G.S.

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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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^a621.13.31^2VINITI
К 90

Культивирование дрожжей на продуктах переработки бурого угля с использованием косубстратов и стимуляторов роста [Текст] : научное издание / Н. С. Печуркин [и др.] // Микробиология. - 1988. - Т. 57, N 5. - С. 892-894 . - ISSN 0026-3656

ГРНТИ

62.13.31

РУБ 621.13.31
Рубрики:
БЕЛОК ОДНОКЛЕТОЧНЫХ
   ДРОЖЖИ
   КУЛЬТИВИРОВАНИЕ
   ПИТАТЕЛЬНАЯ СРЕДА
   ОТХОДЫ
   ПРОМЫШЛЕННЫЕ
   SINGLE CELL PROTEIN
   ЕА Т
   С Т Е
   Т Е Т МЕ М
   В О СОА
   СО В Т АТЕ
   О ТН Т М А Т
   В ОМА
Аннотация: Сделан вывод, что для увеличения выхода биомассы дрожжей, потребляющих субстрат из угля, предпочтительно добавлять такие стимуляторы роста, как аскорбиновая кислота и древесный гидролизат. Библ. 4. Ин-т биофизики СО АН СССР, Красноярск, СССР
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Печуркин, Н.С.; Попова, Л.Ю.; Тушкова, Г.И.; Фуряева, А.В.; Марченкова, Т.В.; Лалетин, А.И.

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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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Green flavoprotein from P. leiognathi: purification, characterization and identification as the product of the lux G(N) gene / A. A. Raibekas // Journal of bioluminescence and chemiluminescence. - 1991. - Vol. 6, Is. 3. - P. 169-176 . - ISSN 0884-3996
Кл.слова (ненормированные):
bacterial protein -- flavoprotein -- amino acid sequence -- article -- bacterial gene -- chemistry -- genetics -- isolation and purification -- luminescence -- molecular genetics -- molecular weight -- Photobacterium -- Amino Acid Sequence -- Bacterial Proteins -- Flavoproteins -- Genes, Bacterial -- Luminescence -- Molecular Sequence Data -- Molecular Weight -- Photobacterium -- Support, U.S. Gov't, P.H.S.
Аннотация: A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.

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

Доп.точки доступа:
Raibekas, A.A.

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THE ENTRY INTO S-PERIOD OF NUCLEI IN HETERODIKARYONS MODIFIED BY THE CYCLOHEXIMIDE [Текст] / N. A. SETKOV, V. N. KAZAKOV, T. V. ANDREEVA // TSITOLOGIYA. - 1991. - Vol. 33, Is. 12. - P. 73-78. - Cited References: 16 . - ISSN 0041-3771

РУБ Cell Biology
Рубрики:
NIH 3T3 CELLS
   DNA-SYNTHESIS
   RESTING CELLS
   C-MYC
   FUSION
   FIBROBLASTS
   EXPRESSION
   GENES
Аннотация: Serum-deprived (0.2%) resting NIH 3T3 mouse fibroblasts were fused with serum-stimulated (10%) proliferating cells to elucidate mechanisms of entering into S-period operating in the nuclei of the heterokaryons under the effect of cycloheximide - an inhibitor of protein synthesis. Using radioautography DNA synthesis was investigated in mono-, homo- and heterodikaryons. After short (0.5-3.0 h) depressing of protein synthesis, the nuclei of stimulated cells in heterokaryons were found to enter into S-period. Under these conditions no induction of DNA synthesis was found in the nuclei of resting cells in heterodikaryons. In other experiments, resting cells were under the effect of cycloheximide during 2-4 h before the fusion, that led to a great induction of DNA synthesis in the nuclei of these cells in heterodikaryons. The data obtained are consistent with the idea of fibroblast transition to the rest under the action of labile proteins-repressors.

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

Доп.точки доступа:
SETKOV, N.A.; KAZAKOV, V.N.; ANDREEVA, T.V.

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^a343.17.09.05^2VINITI
Л 94

Люминесценция Ca{2}{+}-активируемого фотопротеина обелина под действием активных форм кислорода [Текст] : научное издание / Е. С. Высоцкий [и др.] // Докл. АН СССР. - 1991. - Т. 321, N 4. - С. 850-854 . - ISSN 0002-3264

ГРНТИ

34.17.09

РУБ 343.17.09.05
Рубрики:
БЕЛОК
   ОБЕЛИН
   КАЛЬЦИЙ-АКТИВИРУЕМЫЙ
   ЛЮМИНЕСЦЕНЦИЯ
   КИСЛОРОД АКТИВНЫЙ
   КИШЕЧНОПОЛОСТНЫЕ
   PROTEIN
   LUMINESCENCE
   ACTION OXYGEN
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Высоцкий, Евгений Степанович; Бондарь, Владимир Станиславович; Трофимов, К. П.; Гительзон, Иосиф Исаевич

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10.

ISOLATION AND PROPERTIES OF VARIOUS MOLECULAR-FORMS OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN [Текст] / Y. S. VYSOTSKII, V. S. BONDAR, I. I. GITELZON // DOKLADY AKADEMII NAUK SSSR. - 1991. - Vol. 321, Is. 1. - С. 214-217. - Cited References: 14 . - ISSN 0002-3264

РУБ Multidisciplinary Sciences
Рубрики:
CALCIUM-ACTIVATED PHOTOPROTEINS
   CTENOPHORES MNEMIOPSIS SP
   BEROE-OVATA
   AEQUORIN
   PROTEIN
   PURIFICATION
   EXTRACTION
   PHIALIDIN
   SEQUENCE
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
VYSOTSKII, Y.S.; BONDAR, V.S.; GITELZON, I.I.

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11.

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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12.

ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA [Текст] / B. A. ILLARIONOV [и др.] // Dokl. Akad. Nauk. - 1992. - Vol. 326, Is. 5. - С. 911-913. - Cited References: 12 . - ISSN 0869-5652

РУБ Multidisciplinary Sciences
Рубрики:
AEQUORIN
   PROTEIN
   PHIALIDIN
   CLONING
   CA-2+
: 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
ILLARIONOV, B.A.; MARKOVA, S.V.; BONDAR, V.S.; VYSOTSKY, E.S.; GITELSON, J.I.

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13.

PROTEIN-SYNTHESIS INHIBITORS, LIKE GROWTH-FACTORS, MAY RENDER RESTING 3T3 CELLS COMPETENT FOR DNA-SYNTHESIS - A AUTORADIOGRAPHIC AND CELL-FUSION STUDY [Text] / N. A. SETKOV [et al.] // Cell Prolif. - 1992. - Vol. 25, Is. 3. - P. 181-191, DOI 10.1111/j.1365-2184.1992.tb01393.x. - Cited References: 20 . - ISSN 0960-7722

РУБ Cell Biology
Рубрики:
C-MYC
   CYCLOHEXIMIDE
   FIBROBLASTS
   EXPRESSION
   INDUCTION
   GENES
   FOS
Аннотация: Serum-deprived (0.1-0.2%) resting NIH 3T3 mouse fibroblasts pre-incubated with cycloheximide (7.5-mu-g/ml), or puromycin (10-mu-g/ml), were fused with stimulated cells taken 10 h after changing the medium to one containing 10% serum, and DNA synthesis was investigated in the nuclei of monokaryons, homodikaryons and heterodikaryons using radioautography with the double-labelling technique. Pre-incubation of resting cells with inhibitors of protein synthesis for 1-4 h abolished their ability to suppress DNA synthesis in stimulated nuclei in heterokaryons. Three hours after the removal of cycloheximide from the medium, the resting cells acquired once again the inhibitory capacity for entry of stimulated nuclei into the S period. This inhibitory influence disappeared also in the case of post-fusion cycloheximide application as well as following an 8-12 h pre-treatment of resting cells with actinomycin D (1-mu-g/ml) prior to fusion. Pre-incubation of resting cells for 12 h with PDGF (1 u/ml-1) followed by an 8-48 h incubation in serum-free medium stimulated the onset of DNA synthesis. A brief exposure (45 min) of resting cells to cycloheximide (7.5-mu-g/ml), or puromycin (7.5-mu-g/ml), exerted a similar effect, inducing by itself the entry of cells into the S period. The results support the assumption that acquirement, by resting cells, of competence for DNA replication includes as a necessary step the down-regulation of intracellular growth inhibitors whose formation depends on protein synthesis.

WOS
Держатели документа:
ACAD SCI USSR,INST BIOPHYS,KRASNOYARSK,USSR
WA ENGELHARDT MOLEC BIOL INST,MOSCOW,USSR
ИБФ СО РАН : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
SETKOV, N.A.; KAZAKOV, V.N.; ROSENWALD, I.B.; MAKAROVA, G.F.; EPIFANOVA, O.I.

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14.

15.

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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16.

EFFECT OF TEMPERATURE ON ACTIVITY AND STABILITY OF OBELIN [Text] / V. S. BONDAR [et al.] // Biochem.-Moscow. - 1992. - Vol. 57, Is. 7. - P717-724. - Cited References: 15 . - 8. - ISSN 0006-2979

РУБ Biochemistry & Molecular Biology
Рубрики:
CA-2+
PHOTOPROTEINS
INDICATORS
Кл.слова (ненормированные):
PHOTOPROTEINS -- OBELIN -- ACTIVATION ENERGY -- THERMOINACTIVATION -- THERMOSTABILITY
Аннотация: The temperature dependence of bioluminescent activity of the Ca2+-activated photoprotein obelin from the hydroid polyp Obelia longissima and thermoinactivation of this protein at different concentrations of (NH4)2SO4 have been studied. The maximal intensity of luminescence of obelin was observed at 4-15-degrees-C. The activity of the photoprotein is completely stable to storage for 3 days at room temperature. Increasing the temperature to 40-degrees-C resulted in a 25-30% loss of enzyme activity in 1 h. The presence of ammonium sulfate during heating stabilizes the activity of obelin. Two breaks, at 11 +/- 3-degrees-C and 47 +/- 3-degrees-C, are observed in the Arrhenius plot of the first-order rate constant of the luminescence decay. The bioluminescent curves of obelin are biphasic in the temperature range 10-40-degrees-C. It is assumed that obelin may exist in two kinetically distinct conformers (active and inactive) whose ratio is temperature dependent.
: 660036, Красноярск, Академгородок, д. 50, стр. 50

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

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17.

Opportunities and constraints of closed man-made ecological systems on the moon / V. Blum [et al.] // Advances in Space Research. - 1994. - Vol. 14, Is. 6. - P271-280 . - ISSN 0273-1177
Аннотация: Most scenarios for a manned lunar base include a combination of physical-chemical and bioregenerative life support systems. Especially on the lunar surface, however, there is a series of special environmental factors which seriously affect the organisms suitable for food production and biological regeneration of the habitat atmosphere and water. So, e.g. the lunar day/night period creates difficult problems for higher plant culture. The paper presents the current scientific approaches to bioregenerative life support systems of a lunar base and discusses critically the possibilities of their realization. Moreover, a scientific strategy is developed with the biologist's point of view to implement in a stepwise manner bioregenerative life support modules into a lunar base covering the possibilities of the untilization of chemolytotrophic bacteria, microalgae and higher plants as well as those of animal breeding and protein production in intensive aquaculture systems. В© 1994.

Scopus
Держатели документа:
Institute of Biophysics, Russian Academy of Sciences, Krasnoyarsk, Russian Federation
German Aerospace Establishment, Cologne-Porz, Germany
Comparative Endocrinology Research Section, Ruhr-University, Bochum, Germany : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Blum, V.; Gitelson, J.I.; Horneck, G.; Kreuzberg, K.

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18.

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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19.

OKADAIC ACID IS AN INHIBITOR OF TYPE-1 AND TYPE 2A PROTEIN PHOSPHATASES STIMULATED DNA-SYNTHESIS IN RESTING CELLS NIH 3T3 [Текст] / N. A. SETKOV // Dokl. Akad. Nauk. - 1995. - Vol. 340, Is. 1. - P. 114-118. - Cited References: 15 . - ISSN 0869-5652

РУБ Multidisciplinary Sciences
Рубрики:
PHOSPHORYLATION
   NUCLEI
   FUSION
   HETERODIKARYONS
   PROLIFERATION
   FIBROBLASTS
   CYCLIN

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

Доп.точки доступа:
SETKOV, N.A.

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20.

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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