来自鸡肝溶酶体的酸性ATP酶。III. 一种金属离子激活的ATP酶与膜性磷脂酰肌醇结合。

Acid ATPase from chicken liver lysosomes. III. A metal ion-activated ATPase combines with membranous phosphatidylinositol.

作者信息

Maeda K, Ohta Y, Nakabayashi T, Taguchi R, Ikezawa H

出版信息

Biochem Int. 1986 Jun;12(6):855-63.

Abstract

A metal ion-activated acid ATPase was present in chicken liver lysosomes. We used Zn2+ as an activator. Lysosomal extract containing octylglucoside from chicken liver was centrifuged at 100,000 xg for 60 min. The supernatant was analyzed by gel filtration on a Sepharose 6B column. Two peaks of metal ion-activated acid ATPase activities were obtained according to the distribution patterns. Each of the two active fractions was incubated with phosphatidylinositol-specific phospholipase C at 37 degrees C for 60 min. The resulting solution was analyzed by gel filtration on a smaller size column of Sepharose 6B again. Molecular weight of the major peak was altered from approx. 1,600,000 to 130,000, whereas that of the minor one, 700,000, remained unchanged.

摘要

鸡肝溶酶体中存在一种金属离子激活的酸性ATP酶。我们使用Zn2+作为激活剂。将含有来自鸡肝的辛基葡糖苷的溶酶体提取物在100,000 xg下离心60分钟。通过在Sepharose 6B柱上进行凝胶过滤分析上清液。根据分布模式获得了两个金属离子激活的酸性ATP酶活性峰。将两个活性级分中的每一个与磷脂酰肌醇特异性磷脂酶C在37℃下孵育60分钟。再次通过在较小尺寸的Sepharose 6B柱上进行凝胶过滤分析所得溶液。主峰的分子量从约1,600,000变为130,000，而次要峰的分子量700,000保持不变。