Lefebvre Y A, White D A, Hawthorne J N
Can J Biochem. 1976 Aug;54(8):746-53. doi: 10.1139/o76-106.
(1) A phosphatidylinositol kinase (EC 2.7.1.67) of a chromaffin vesicle membrane preparation isolated from bovine adrenal medulla was characterized. Its activity towards endogenous and exogenous phosphatidylinositol was very similar to the kinase activity of the microsomal fraction prepared from the same tissue. (2) Phosphomonoesterase (EC 3.1.3.36) and diesterase activity hydrolysing membrane bound phosphatidylinositol 4-phosphate was located mainly in the microsomal fraction. No hydrolytic activity was present in the vesicle membrane. (3) Phosphorylation of chromaffin vesicle membrane phosphatidylinositol did not increase calcium-binding by the membranes.
(1) 对从牛肾上腺髓质分离得到的嗜铬囊泡膜制剂中的磷脂酰肌醇激酶(EC 2.7.1.67)进行了特性鉴定。其对内源性和外源性磷脂酰肌醇的活性与从同一组织制备的微粒体部分的激酶活性非常相似。(2) 水解膜结合的磷脂酰肌醇4-磷酸的磷酸单酯酶(EC 3.1.3.36)和二酯酶活性主要位于微粒体部分。囊泡膜中不存在水解活性。(3) 嗜铬囊泡膜磷脂酰肌醇的磷酸化并未增加膜对钙的结合。