大鼠肾皮质的磷脂酰肌醇激酶和二磷酸肌醇激酶：特性与亚细胞定位
Phosphatidylinositol kinase and diphosphoinositide kinase of rat kidney cortex: properties and subcellular localization.
作者信息
Cooper P H, Hawthorne J N
出版信息
Biochem J. 1976 Oct 15;160(1):97-105. doi: 10.1042/bj1600097.
Abstract
The properties of phosphatidylinositol kinase and diphosphoinositide kinase from rat kidney cortex were studied. The enzymes were completely Mg2+-dependent. Cutscum detergent activated phosphatidylinositol kinase, but diphosphoinositide kinase was inhibited by all detergents tested. The pH optima were 7.7 for phosphatidylinositol kinase and 6.5 for diphosphoinositide kinase. On subcellular fractionation of kidney-cortex homogenates by differential centriflgation, the distribution of phosphatidylinositol kinase resembled that of the marker enzymes for brush-border, endoplasmic-reticulum and Golgi membranes. Diphosphoinositide kinase distribution resembled that of thiamin pyrophosphatase (assayed in the absence of ATP), diphosphoinositide phosphatase and triphosphoinositide phosphatase. Activities of both kinases were low in purified brush-border fragments. Diphosphoinositide kinase is probably localized in the Golgi complex.
摘要
对大鼠肾皮质中的磷脂酰肌醇激酶和二磷酸肌醇激酶的特性进行了研究。这些酶完全依赖Mg2+。曲通去污剂可激活磷脂酰肌醇激酶，但二磷酸肌醇激酶受到所有测试去污剂的抑制。磷脂酰肌醇激酶的最适pH值为7.7，二磷酸肌醇激酶的最适pH值为6.5。通过差速离心对肾皮质匀浆进行亚细胞分级分离时，磷脂酰肌醇激酶的分布类似于刷状缘、内质网和高尔基体膜的标志酶的分布。二磷酸肌醇激酶的分布类似于硫胺素焦磷酸酶（在无ATP的情况下测定）、二磷酸肌醇磷酸酶和三磷酸肌醇磷酸酶的分布。在纯化的刷状缘片段中，两种激酶的活性都很低。二磷酸肌醇激酶可能定位于高尔基体复合体中。
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