Williams J T, Juo P S
Biochim Biophys Acta. 1976 Jan 23;422(1):120-6. doi: 10.1016/0005-2744(76)90013-9.
A sedimentable form of acid phosphatase (EC 3.1.3.2) from Tetrahymena pyriformis was found to be solubilized by Triton X-100. The total enzyme activity in the insoluble cell fraction increased almost 200% upon solubilization with Triton X-100 or Nonidet P-40. Removal of membrane lipids and Triton X-100 from the particulate wash solution with a chloroform extraction resulted in non-specific enzyme-protein aggregation which was reversible upon addition of Triton X-100. The results indicate that this acid phosphatase is an integral membrane protein. The pH optima for this particulate bound acid phosphatase was 3.5 with o-carboxyphenyl phosphate and 4.0 with p-nitrophenyl phosphate as substrates. The Km values of each substrate were 3.1 and 0.031 mM, respectively.
发现来自梨形四膜虫的一种可沉降形式的酸性磷酸酶（EC 3.1.3.2）可被 Triton X - 100 溶解。用 Triton X - 100 或 Nonidet P - 40 溶解后，不溶性细胞组分中的总酶活性增加了近 200%。用氯仿萃取从颗粒洗涤溶液中去除膜脂和 Triton X - 100 会导致非特异性酶 - 蛋白聚集，添加 Triton X - 100 后这种聚集是可逆的。结果表明这种酸性磷酸酶是一种整合膜蛋白。以邻羧基苯磷酸和对硝基苯磷酸为底物时，这种颗粒结合酸性磷酸酶的最适 pH 分别为 3.5 和 4.0。每种底物的 Km 值分别为 3.1 和 0.031 mM。
