Properties of human erythrocyte phosphatidylinositol kinase and inhibition by adenosine, ADP and related compounds.
Properties of human erythrocyte phosphatidylinositol kinase and inhibition by adenosine, ADP and related compounds.
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人红细胞磷脂酰肌醇激酶的特性以及腺苷、ADP 和相关化合物的抑制作用。
DOI：
10.1016/0304-4165(77)90081-2
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发表时间：
1977
期刊：
影响因子：
--
通讯作者：
J. Buckley
中科院分区：
文献类型：
--
作者：
J. Buckley
1. An improved assay for the enzyme phosphatidylinositol kinase is described. The kinase activity is increased more than 10-fold by the addition of mercaptoethanol and exogenous phosphatidylinositol in the presence of Triton X-100. The enzyme is solubilized by non-ionic detergents. 2. Phosphatidylinositol kinase is inhibited by physiological concentrations of ADP and by similar levels of adenosine. Cyclic AMP, AMP and theophylline inhibit at higher concentrations. Caffeine is much less effective than theophylline as an inhibitor. Guanine nucleotides do not appreciably inhibit the kinase. All the inhibitors tested seemed to compete with ATP. Theophylline also reduced the rate of polyphosphoinositide synthesis in intact cells. 3. Possible roles of polyphosphoinositides in energy charge maintenance and inversion and resealing are discussed.
