The presence of Ca2+-independent phospholipase A1 highly specific for phosphatidylinositol in bovine brain

Hiroshi Ueda, Tetsuyuki Kobayashi*, Masaaki Kishimoto, Tomonari Tsutsumi, Shiro Watanabe, Harumi Okuyama

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

22 被引用数 (Scopus)

抄録

EDTA-insensitive phospholipase A activity hydrolyzing phosphatidylinositol was detected in a bovine brain soluble fraction. This phospholipase A was purified 25-fold by sequential chromatographies of DEAE-Toyopearl, Phenyl-Toyopearl, and Ultrahydrogel 1000. The partially purified EDTA-insensitive phospholipase A showed an apparent molecular mass of 230kDa on an Ultrahydrogel 1000 column in the presence of 0.05% Triton X-100 and a pH optimum at 7.0. The enzyme was highly specific for phosphatidylinositol; phosphatidylethanolamine and phosphatidylcholine were not hydrolyzed significantly. The enzyme activity was characterized as phospholipase A1, and Ca2+ and Mg2+ were not required for its activity. These results indicate the existence of Ca2+-independent, phosphatidylinositol-specific metabolism besides those catalyzed by Ca2+-dependent phospholipase A2 and Ca2+-dependent, phosphatidylinositol-specific phospholipase C.

本文言語英語
ページ(範囲)1272-1279
ページ数8
ジャーナルBiochemical and Biophysical Research Communications
195
3
DOI
出版ステータス出版済み - 1993/09/30

ASJC Scopus 主題領域

  • 生物理学
  • 生化学
  • 分子生物学
  • 細胞生物学

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