Ecto-ATP diphosphohydrolase (apyrase) in ovarian follicle cells of starfish Asterina pectinifera

Masatoshi Mita, Michiyasu Yoshikuni, Yoshitaka Nagahama

研究成果: Contribution to journalArticle査読

8 被引用数 (Scopus)

抄録

A Mg2+-dependent ecto-ATP diphosphohydrolase (ATPDase, EC 3.6.1.5) was present in starfish ovarian follicle cells. The enzyme which had an optimum pH between 6.0 and 7.5 could hydrolyze triphosphonucleosides (ATP, dATP, GTP, CTP, UTP and ITP) and diphosphonucleosides (ADP, dADP, GDP, CDP, UDP and IDP), but not monophosphonucleosides. The K(m) values for ATP and ADP were 0.17 and 0.20 mM, respectively. The ATPDase activity was insensitive to specific ATPase inhibitors, such as ouabain, vanadate and oligomycin, an adenylate kinase inhibitor, P1, P5-di-(adenosine-5')pentaphosphate, and a phosphodiesterase inhibitor, 1-isobutyl-3-methylxanthine. The activity was mostly distributed in the membrane fraction of follicle cells. It is also interesting that hydrolysis of ATP and ADP occurred upon incubation of intact cells in seawater. Among various kinds of detergents, digitonin was capable of solubilizing the enzyme from the membrane fraction. Using digitonin extract, a high-performance liquid chromatography with Superose 6 column showed that the molecular weight of ecto-ATPDase in starfish follicle cells was ~60 000. Copyright (C) 1998 Elsevier Science Inc.

本文言語英語
ページ(範囲)577-583
ページ数7
ジャーナルComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
119
3
DOI
出版ステータス出版済み - 1998
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 生理学
  • 分子生物学

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