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1.

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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2.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., MARKOVA S.V., BONDAR V.S., VYSOTSKY E.S., GITELSON J.I.
Заглавие : ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA
Колич.характеристики :3 с
Место публикации : Dokl. Akad. Nauk: MEZHDUNARODNAYA KNIGA, 1992. - Vol. 326, Is. 5. - С. 911-913. - ISSN 0869-5652
Примечания : Cited References: 12
Предметные рубрики: AEQUORIN
PROTEIN
PHIALIDIN
CLONING
CA-2+
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3.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : ILLARIONOV B.A., MARKOVA S.V., BONDAR V.S., VYSOTSKY E.S., GITELSON J.I.
Заглавие : ISOLATION AND EXPRESSION OF CDNA CODING FOR PHOTOPROTEIN OBELIN FROM HYDROID OBELIA-LONGISSIMA
Место публикации : Dokl. Akad. Nauk: MEZHDUNARODNAYA KNIGA, 1992. - Vol. 326, Is. 5. - С. 911-913. - 3. - ISSN 0869-5652
Примечания : Cited References: 12
Предметные рубрики: AEQUORIN
PROTEIN
PHIALIDIN
CLONING
CA-2+
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4.

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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5.

Вид документа : Статья из журнала
Шифр издания :
Автор(ы) : BONDAR V.S., TROFIMOV K.P., SANDALOV T.P., VYSOTSKII E.S.
Заглавие : EFFECT OF TEMPERATURE ON ACTIVITY AND STABILITY OF OBELIN
Место публикации : Biochem.-Moscow: PLENUM PUBL CORP, 1992. - Vol. 57, Is. 7. - С. 717-724. - 8. - ISSN 0006-2979
Примечания : Cited References: 15
Предметные рубрики: CA-2+
PHOTOPROTEINS
INDICATORS
Ключевые слова (''Своб.индексиров.''): 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.
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