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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Бондарь В.С., Высоцкий Е.С., Рожманова О.М., Воронина С.Г.
Заглавие : Ca{2+}-активируемый фотопротеин обелин как индикатор кальциевого транспорта в протеолипосомах, включающих мембраны Т-системы скелетных мышц : научное издание
Место публикации : Биохимия. - 1991. - Т. 56, N 5. - С. 806-811. - ISSN 0320-9725
ГРНТИ : 34.17.27
Предметные 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
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKII Y.S., BONDAR V.S., GITELZON I.I.
Заглавие : ISOLATION AND PROPERTIES OF VARIOUS MOLECULAR-FORMS OF CA2+-ACTIVATED PHOTOPROTEIN OBELIN
Колич.характеристики :4 с
Место публикации : DOKLADY AKADEMII NAUK SSSR: MEZHDUNARODNAYA KNIGA, 1991. - Vol. 321, Is. 1. - С. 214-217. - ISSN 0002-3264
Примечания : Cited References: 14
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
PROTEIN
PURIFICATION
EXTRACTION
PHIALIDIN
SEQUENCE
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., VYSOTSKII E.S., ROZHMANOVA O.M., VORONINA S.G.
Заглавие : THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN AS AN INDICATOR OF CALCIUM-TRANSPORT IN PROTEOLIPOSOMES CONTAINING MEMBRANES OF THE T-SYSTEM OF SKELETAL-MUSCLES
Колич.характеристики :5 с
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1991. - Vol. 56, Is. 5. - С. 546-550. - ISSN 0006-2979
Примечания : Cited References: 12
Предметные рубрики: CHANNEL
CA-2+
MODULATION
BINDING
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., TROFIMOV K.P., VYSOTSKII E.S.
Заглавие : PHYSICOCHEMICAL PROPERTIES OF A PHOTOPROTEIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 10. - С. 1020-1027. - 8. - ISSN 0006-2979
Примечания : Cited References: 36
Предметные рубрики: CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
BEROE-OVATA
AEQUORIN
CA-2+
INDICATORS
PROTEIN
BINDING
PURIFICATION
EXTRACTION
Ключевые слова (''Своб.индексиров.''): bioluminescence--ca2+-activated photoprotein--obelin--chromatography--calcium
Аннотация: The photoprotein obelin was isolated and purified to homogeneity (as indicated by sodium dodecyl sulfate polyacrylamide gel electrophoresis) from hydroids of Obelia longissima by gel filtration on Sephadex G-75 fine, ion exchange chromatography on Polysil CA-300 (10 mum), hydrophobic chromatography on Phenyl-Sepharose CL-4B, gel filtration on Sephacryl S-200 superfine, ion exchange chromatography on a Mono Q column at pH 7.0, chromatofocusing on a Mono P column (pH gradient 6.0-4.0), and ion exchange chromatography on a Mono Q column at pH 5.5, 8.8, and 7.0. The molecular weight of the native protein was 30 kD, and that measured in the presence of SDS was 19.8 kD. The specific activity of obelin is 4.9.10(15) quanta/mg protein, pseudo-first-order constant of bioluminescence decay 4 sec-1, and quantum yield 0.16 The range of measurable Ca2+ concentrations is 10(-7) to 10(-5) M. The luminescence spectrum of obelin peaks at 469 nm, and the fluorescence emission maximum of the discharged protein is at 455 nm. The optimum pH for luminescence is between 9.0 and 10.5. The molecular ionization constants are pK1 6.8 and pK2 12.2, and the ionization constants for the active site are pK1 9.1 and pK2 10.2
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Trofimov K.P., Bondar' V.S., Gitelson J.I.
Заглавие : Luminescence of Ca(2+)-activated photoprotein obelin initiated by NaOCl and MnCl2.
Место публикации : Journal of bioluminescence and chemiluminescence. - 1993. - Vol. 8, Is. 6. - С. 301-305. - ISSN 08843996 (ISSN)
Ключевые слова (''Своб.индексиров.''): 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
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., BONDAR V.S., ILLARIONOVA V.A., VYSOTSKI E.S.
Заглавие : SEQUENCE OF THE CDNA-ENCODING THE CA2+-ACTIVATED PHOTOPROTEIN OBELIN FROM THE HYDROID POLYP OBELIA-LONGISSIMA
Место публикации : Gene: ELSEVIER SCIENCE BV, 1995. - Vol. 153, Is. 2. - С. 273-274. - 2. - ISSN 0378-1119, DOI 10.1016/0378-1119(94)00797-V
Примечания : Cited References: 6
Предметные рубрики: CA-2+-ACTIVATED PHOTOPROTEIN
AEQUORIN
CLONING
Ключевые слова (''Своб.индексиров.''): 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : MATVEEV S.V., ILLARIONOV B.A., VYSOTSKI E.S., BONDAR V.S., MARKOVA S.V., ALAKHOV Y.B.
Заглавие : OBELIN MESSENGER-RNA - A NEW TOOL FOR STUDIES OF TRANSLATION IN CELL-FREE SYSTEMS
Колич.характеристики :6 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1995. - Vol. 231, Is. 1. - С. 34-39. - ISSN 0003-2697, DOI 10.1006/abio.1995.1499
Примечания : Cited References: 17
Предметные рубрики: MESSENGER-RNA
AEQUORIN
PROTEIN
CLONING
CDNA
Аннотация: Obelin mRNA obtained in vitro with the aid of SP6 RNA polymerase was translated in a wheat germ cell-free system, Only the polypeptide with a molecular mass of about 20 kDa was synthesized. The activation of apoobelin with a synthetic coelenterazine revealed a luminescence activity initiated by calcium. The specific activity was 3.6 +/- 0.4 x 10(15) photons per mg of the in vitro synthesized obelin (k = 6.9 s(-1)). The luminescence of the obelin was in a good correlation with the protein concentration calculated by the incorporation of [C-14]Leu. The determination of the amount of de novo synthesized obelin based on measurement of its luminescence is one-thousand times more sensitive than the approach based on the incorporation of labeled amino acid. Thus, obelin mRNA has some advantages for evaluating the efficiency of cell-free translation when compared with standard methods. (C) 1995 Academic Press, Inc.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : VYSOTSKI E.S., TROFIMOV C.P., BONDAR V.S., FRANK L.A., MARKOVA S.V., ILLARIONOV B.A.
Заглавие : MN2+-ACTIVATED LUMINESCENCE OF THE PHOTOPROTEIN OBELIN
Место публикации : Arch. Biochem. Biophys.: ACADEMIC PRESS INC JNL-COMP SUBSCRIPTIONS, 1995. - Vol. 316, Is. 1. - С. 92-99. - 8. - ISSN 0003-9861, DOI 10.1006/abbi.1995.1014
Примечания : Cited References: 38
Предметные 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.
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Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Bondar V.S.
Заглавие : On possible biological function of cadmium as analog of calcium
Колич.характеристики :2 с
Место публикации : Dokl. Akad. Nauk: MEZHDUNARODNAYA KNIGA, 1997. - Vol. 352, Is. 5. - С. 693-694. - ISSN 0869-5652
Примечания : Cited References: 12
Предметные рубрики: PHOTOPROTEIN OBELIN
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10.

Вид документа : Статья из сборника (однотомник)
Шифр издания :
Автор(ы) : Illarionova V.A., Illarionov B.A., Bondar V.S., Vysotski E.S., Blinks J.R.
Заглавие : 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
Место публикации : BIOLUMINESCENCE AND CHEMILUMINESCENCE: MOLECULAR REPORTING WITH PHOTONS: JOHN WILEY & SONS LTD, 1997. - 9th International Symposium on Bioluminescence and Chemiluminescence (OCT, 1996, WOODS HOLE, MA). - С. 431-434. - 4. - ISBN 0-471-97502-8
Примечания : Cited References: 0
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11.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Manukovsky N.S., Kovalev V.S., Gribovskaya I.V.
Заглавие : Utilization of substrate when growing oyster mushroom Pleurotus florida Fovose
Колич.характеристики :4 с
Место публикации : Mikol. Fitopatol.: MEZHDUNARODNAYA KNIGA, 1998. - Vol. 32, Is. 6. - P43-46. - ISSN 0026-3648
Примечания : Cited References: 8
Аннотация: Content of biogenic elements in the residual substrate after growing of oyster mushroom Pleurotus florida Fovose on wheat straw was studied. It was calculated, that masses of sulphur, calcium and magnesium in the residual substrate were more than 90 % of their initial masses in wheat straw used for growing. Therefore the accumulation of these elements in the substrate under its repeated recycling for mushroom growing is possible. On the contrary the lack of phosphorus is expected. After washing content of all biogenic elements tested in residual substrate, except for calcium, was lower than their content in wheat straw. The decreasing of mushroom yield under increasing rate of residual substrate in its mixture with wheat straw was shown. Washing of residual substrate did not lead to decreasing of yield.
WOS
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12.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Berestovskaya N.G., Shaloiko L.A., Gorokhovatsky A.Y., Bondar V.S., Vysotski E.S., Maximov J.E., von Doehren H..., Alakhov Y.B.
Заглавие : Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC, 1999. - Vol. 268, Is. 1. - P72-78. - ISSN 0003-2697, DOI 10.1006/abio.1998.3051
Примечания : Cited References: 22
Предметные рубрики: SEQUENCE-ANALYSIS
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
LIGHT-EMISSION
AEQUORIN
CDNA
CLONING
EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.
WOS
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13.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Berestovskaya N.G., Shaloiko L.A., Gorokhovatsky A.Y., Bondar V.S., Vysotski E.S., Maximov J.E., von Doehren H..., Alakhov Y.B.
Заглавие : Cotranslational formation of active photoprotein obelin in a cell-free translation system: Direct ultrahigh sensitive measure of the translation course
Колич.характеристики :7 с
Место публикации : Anal. Biochem.: ACADEMIC PRESS INC, 1999. - Vol. 268, Is. 1. - С. 72-78. - ISSN 0003-2697, DOI 10.1006/abio.1998.3051
Примечания : Cited References: 22
Предметные рубрики: SEQUENCE-ANALYSIS
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
LIGHT-EMISSION
AEQUORIN
CDNA
CLONING
EXPRESSION
Аннотация: Translation of apoobelin mRNA in a cell-free wheat germ translation system in the presence of coelenterazine and molecular oxygen results in cotranslational formation of active photoprotein. Active obelin formation is recorded by its luminescence, either direct in the translation mixture in the presence of coelenterazine and calcium ions or in aliquots from the translation mixture. In the second case translation is carried out with coelenterazine and EGTA. Registration of the translation course by luminescence of the synthesized product in both cases allows use of apoobelin mRNA at very low concentrations as an internal marker for immediate measure of protein biosynthesis activity of in vitro translation systems. It is shown that the simultaneous translation of any other mRNA does not affect translation of photoprotein mRNAs under standard conditions. Continuous registration of luminescence in a cuvette of a liquid scintillation counter in photon-counting mode varies the time of signal accumulation in a wide temporal range, thus increasing the numerical values of the recorded signals. Registration of photoprotein luminescence during translation can be used to obtain additional information about the translation process, for example codon reading speed, about protein folding, and about the formation of active proteins on ribosomes. (C) 1999 Academic Press.
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14.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Liu Z.J., Rose J..., Wang B.C., Lee J...
Заглавие : Preparation and preliminary study of crystals of the recombinant calcium-regulated photoprotein obelin from the bioluminescent hydroid Obelia longissima
Колич.характеристики :2 с
Место публикации : Acta Crystallogr. Sect. D-Biol. Crystallogr.: MUNKSGAARD INT PUBL LTD, 1999. - Vol. 55. - С. 1965-1966. - ISSN 0907-4449, DOI 10.1107/S0907444999011828
Примечания : Cited References: 23
Предметные рубрики: AEQUORIN
LUCIFERASE
LIGHT
Аннотация: Crystals of recombinant obelin, the Ca2+-regulated photoprotein from the marine hydroid Obelia longissima, have been grown from sodium citrate solutions. Crystals grow as hexagonal light-yellow rods (0.1 x 0.1 x 1.0 mm) which diffract to beyond 1.8 Angstrom with synchrotron radiation of 1.0 Angstrom wavelength. The crystals have a primitive hexagonal lattice with unit-cell parameters a = 81.55, c = 86.95 Angstrom. The asymmetric unit contains two molecules. This represents the successful preparation of single crystals of a photoprotein obelin which have promising diffraction properties.
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15.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Liu Z.J., Vysotski E.S., Chen C.J., Rose J.P., Lee J..., Wang B.C.
Заглавие : Structure of the Ca2+-regulated photoprotein obelin at 1.7 angstrom resolution determined directly from its sulfur substructure
Колич.характеристики :9 с
Место публикации : Protein Sci.: CAMBRIDGE UNIV PRESS, 2000. - Vol. 9, Is. 11. - С. 2085-2093. - ISSN 0961-8368
Примечания : Cited References: 41
Предметные рубрики: CALCIUM-MODULATED PROTEINS
AMINO-ACID SEQUENCE
CA-2+-BINDING PHOTOPROTEIN
CA2+-BINDING PHOTOPROTEIN
MACROMOLECULAR STRUCTURES
3-DIMENSIONAL STRUCTURE
ANOMALOUS SCATTERING
CRYSTAL-STRUCTURES
DIFFRACTION DATA
BINDING SITE
Ключевые слова (''Своб.индексиров.''): bioluminescence--crystallography--obelin--photoprotein--single wavelength anomalous scattering--solvent flattening--sulfur phasing
Аннотация: The crystal structure of the photoprotein obelin (22.2 kDa) from Obelia longissima has been determined and refined to 1.7 Angstrom resolution. Contrary to the prediction of a peroxide, the noncovalently bound substrate, coelenterazine, has only a single oxygen atom bound at the C2-position. The protein-coelenterazine 2-oxy complex observed in the crystals is photo-active because, in the presence of calcium ion, bioluminescence emission within the crystal is observed. This structure represents only the second de novo protein structure determined using the anomalous scattering signal of the sulfur substructure in the crystal. The method used here is theoretically different from that used for crambin in 1981 (4.72 kDa) and represents a significant advancement in protein crystal structure determination.
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16.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Illarionov B.A., Frank L.A., Illarionova V.A., Bondar V.S., Vysotski E.S., Blinks J.R.
Заглавие : Recombinant obelin: Cloning and expression of cDNA, purification, and characterization as a calcium indicator
Колич.характеристики :27 с
Место публикации : Methods Enzymol.: ACADEMIC PRESS INC, 2000. - Vol. 305. - С. 223-249. - ISSN 0076-6879
Примечания : Cited References: 58
Предметные рубрики: PHOTOPROTEIN OBELIN
MESSENGER-RNA
CA-2+-ACTIVATED PHOTOPROTEIN
DIRECTED MUTAGENESIS
SEQUENCE-ANALYSIS
HYDROID OBELIA
AEQUORIN
PROTEIN
BIOLUMINESCENCE
LUMINESCENCE
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17.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Gladyshev M.I., Gribovskaya I.V., Moskvicheva A.V., Muchkina E.Y., Chuprov S.M., Ivanova E.A.
Заглавие : Content of metals in compartments of ecosystem of a Siberian pond
Место публикации : Archives of Environmental Contamination and Toxicology. - 2001. - Vol. 41, Is. 2. - С. 157-162. - ISSN 00904341 (ISSN) , DOI 10.1007/s002440010233
Ключевые слова (''Своб.индексиров.''): 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.
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18.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Vysotski E.S., Liu Z.J., Rose J..., Wang R.C., Lee J...
Заглавие : Preparation and X-ray crystallographic analysis of recombinant obelin crystals diffracting to beyond 1.1 angstrom
Колич.характеристики :3 с
Место публикации : Acta Crystallogr. Sect. D-Biol. Crystallogr.: MUNKSGAARD INT PUBL LTD, 2001. - Vol. 57. - С. 1919-1921. - ISSN 0907-4449, DOI 10.1107/S0907444901016523
Примечания : Cited References: 16
Предметные рубрики: PHOTOPROTEIN AEQUORIN
LONGISSIMA
EVOLUTION
CDNA
Аннотация: Crystals of recombinant obelin, the Ca2+-regulated photoprotein from the marine hydroid Obelia longissima, have been grown from a solution containing PEG 8000 and potassium phosphate. Hexamine-cobalt trichloride was used as an additive to increase the chance of crystallization. The crystals grow in a light yellow cubic form (0.5 x 0.5 x 0.45 mm) which diffracts to beyond 1.1 Angstrom resolution. The crystals belong to the space group C2, with unit-cell parameters a=83.43, b=54.92, c=52.99 Angstrom, beta = 112.00 degrees. The asymmetric unit contains one molecule. Crystals exposed to calcium ion before and after X-ray irradiation emit light, confirming that the crystals consist of an active photoprotein.
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19.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Deng L..., Vysotski E.S., Liu Z.J., Markova S.V., Malikova N.P., Lee J..., Rose J..., Wang B.C.
Заглавие : Structural basis for the emission of violet bioluminescence from a W92F obelin mutant
Колич.характеристики :5 с
Место публикации : FEBS Lett.: ELSEVIER SCIENCE BV, 2001. - Vol. 506, Is. 3. - С. 281-285. - ISSN 0014-5793, DOI 10.1016/S0014-5793(01)02937-4
Примечания : Cited References: 15
Предметные рубрики: AEQUORIN
Ключевые слова (''Своб.индексиров.''): calcium-regulated photoprotein--x-ray crystallography--fluorescence--coelenterazine--aequorin
Аннотация: Mutation of the Trp92 that is known to lie within the active site of the photoprotein obelin from Obelia longissima, results in a shift of the bioluminescence color from blue (lambda (max) = 485 nm) to violet. The corrected spectrum shows a new band with lambda (max) = 410 nm now contributing equally to the one at longer wavelength. The crystal structure of this W92F obelin determined at 1.72 Angstrom resolution shows that there is no significant change in the dimensions of the active site between WT obelin (recombinant Ca2+-regulated photoprotein from Obelia longissima) and the mutant. It is proposed that the bioluminescence spectral shift results from removal of a hydrogen bond from the indole of W92 nearby a hydroxyl belonging to the 6-phenyl substituent of the substrate coelenterazine. Propagation of fbis change through a conjugated bond system in the excited state of the product coelenteramide affects the coupling of the N1-position and the hydrogen-bonded Y138. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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20.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : Markova S.V., Vysotski E.S., Blinks J.R., Burakova L.P., Wang B.C., Lee J...
Заглавие : Obelin from the bioluminescent marine hydroid Obelia geniculata: Cloning, expression, and comparison of some properties with those of other Ca2+-regulated photoproteins
Колич.характеристики :10 с
Место публикации : Biochemistry: AMER CHEMICAL SOC, 2002. - Vol. 41, Is. 7. - С. 2227-2236. - ISSN 0006-2960, DOI 10.1021/bi0117910
Примечания : Cited References: 54
Предметные рубрики: AMINO-ACID-SEQUENCE
CALCIUM-ACTIVATED PHOTOPROTEINS
CTENOPHORES MNEMIOPSIS SP
CA-2+-ACTIVATED PHOTOPROTEIN
LUMINESCENT PROTEIN
BINDING-PROTEIN
BEROE-OVATA
AEQUORIN
CDNA
PURIFICATION
Аннотация: A cDNA encoding the Ca2+-regulated photoprotein of the bioluminescent marine hydroid Obelia geniculata was cloned and sequenced. The cDNA is a 774 bp fragment containing two overlapping open reading frames, one of which contained 585 bp encoding a 195 amino acid polypeptide which obviously has the primary structure of the apoprotein of a calcium-regulated photoprotein. Many of the residues are identical to those in other Ca2+-regulated photoproteins: 86% compared with that from Obelia longissima, 76% with that from Clytia (Phialidium), 64% with that from Aequorea, and 64% with that from Mitrocoma (Halistaura). The obelin from O. geniculata was overexpressed in Escherichia coli, refolded from inclusion bodies, and purified. The yield of highly purified recombinant protein was 55-80 mg/L of LB medium. O. geniculata obelin has absorption maxima at 280 and 460 nm and a shoulder at approximately 310 nm. The calcium-discharged protein loses visible absorption but exhibits a new absorption maximum at 343 nm. The bioluminescence of the obelin from O. geniculata is blue (lambda(max) = 495 nm). In contrast, the fluorescence of the calcium-discharged protein is yellow-green (lambda(max) = 520 nm; excitation at 340 nm). This is in sharp contrast to aequorin in which the bioluminescence and fluorescence emission spectra of the calcium-discharged protein are almost identical (lambda(max) = 465 nm). The Ca2+ concentration-effect curve for O. geniculata obelin is similar to those of many other photoproteins: at [Ca2+] below approximately 10(-8) M, calcium-independent luminescence is observed, and at [Ca2+] approximately 10(-3) M, the luminescence reaches a maximum. Between these extremes, the curve spans a vertical range of almost 8 log units with a maximum slope on a log-log plot of about 2.5. In the absence of Mg2+ the rate constant for the rise of bioluminescence determined by the stopped-flow technique is about 450 s(-1). The effects of Mg2+ on the kinetics of bioluminescence are complicated, but at all concentrations studied they are relatively small compared to the corresponding effects on aequorin luminescence. At least with respect to speed and sensitivity to Mg2+, the obelins from both O. longissima and O. geniculata would appear to be more suitable than aequorin for use as intracellular Ca2+ indicators.
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