De Metz M, Lebret M, Enouf J, Lévy-Tolédano S
Biochim Biophys Acta. 1984 Mar 14;770(2):159-65. doi: 10.1016/0005-2736(84)90125-1.
The phospholipid requirement of the (Ca2+ + Mg2+)-ATPase present in a membrane fraction from human platelets was studied using various purified phospholipases. Only those phospholipases, which hydrolyse the negatively charged phospholipids, inhibited the (Ca2+ + Mg2+)-ATPase activity. The ATPase activity could be restored by adding mixed micelles of Triton X-100 and phosphatidylserine or phosphatidylinositol. Micelles with phosphatidic acid, phosphatidylcholine, phosphatidylethanolamine or sphingomyelin could not be used for reconstitution and inhibited the activity of the native enzyme.
利用各种纯化的磷脂酶研究了人血小板膜组分中存在的(Ca2+ + Mg2+)-ATP酶对磷脂的需求。只有那些能水解带负电荷磷脂的磷脂酶才会抑制(Ca2+ + Mg2+)-ATP酶的活性。通过添加Triton X-100与磷脂酰丝氨酸或磷脂酰肌醇的混合胶束,可以恢复ATP酶的活性。含有磷脂酸、磷脂酰胆碱、磷脂酰乙醇胺或鞘磷脂的胶束不能用于重组,并且会抑制天然酶的活性。