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鸡红细胞中由磷酸单酯酶活性引起的钙离子诱导的多磷酸肌醇分解。

Ca2+-induced polyphosphoinositide breakdown due to phosphomonoesterase activity in chicken erythrocytes.

作者信息

Raval P J, Allan D

出版信息

Biochem J. 1985 Oct 1;231(1):179-83. doi: 10.1042/bj2310179.

Abstract

Treatment of chicken erythrocytes with ionophore A23187 and Ca2+ caused the breakdown of a large proportion of the cellular polyphosphoinositides. Since no diacylglycerol or phosphatidate was generated, but there was a small increase in the level of phosphatidylinositol, it was concluded that breakdown occurred as a result of phosphomonoesterase activation. Experiments with subcellular fractions showed that the phosphomonoesterase activity was present in the cytosolic fraction of the cells.

摘要

用离子载体A23187和Ca2+处理鸡红细胞,导致细胞中大部分多磷酸肌醇分解。由于未生成二酰基甘油或磷脂酸,但磷脂酰肌醇水平略有升高,因此得出结论,分解是磷酸单酯酶激活的结果。亚细胞组分实验表明,磷酸单酯酶活性存在于细胞的胞质组分中。

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本文引用的文献

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The enzymology of stimulated inositol lipid turnover.刺激的肌醇脂质周转的酶学
Cell Calcium. 1982 Oct;3(4-5):295-309. doi: 10.1016/0143-4160(82)90018-5.

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