鲤鱼肝脏酸性磷酸酶的异质性研究：酸性磷酸酶-I。亚基结构和碳水化合物组成。

Studies of the heterogeneity of carp liver acid phosphatases: acid phosphatase--I. Subunit structure and carbohydrate composition.

作者信息

Jańska H, Kubicz A

出版信息

Comp Biochem Physiol B. 1985;82(3):563-7. doi: 10.1016/0305-0491(85)90024-0.

Abstract

The three molecular forms of the carp liver acid phosphatase (AcPase) were shown to be dimeric proteins, two of them differing in molecular weights. An activating effect of ConA binding on the AcPases has been observed. AcPase I and AcPase II showed a mol. wt of 122,500 and of 58,884 +/- 3000 for their subunits. It is assumed that AcPase I is a sialylated derivative of AcPase II. AcPase III has a mol. wt of 93,132 and the two subunits of 46,556 +/- 4000. A homogeneous AcPase I was obtained and its carbohydrate composition is presented.

摘要

鲤鱼肝脏酸性磷酸酶（AcPase）的三种分子形式被证明是二聚体蛋白，其中两种分子量不同。已观察到伴刀豆球蛋白A（ConA）结合对AcPase具有激活作用。AcPase I和AcPase II的亚基分子量分别为122,500和58,884±3000。推测AcPase I是AcPase II的唾液酸化衍生物。AcPase III的分子量为93,132，其两个亚基的分子量为46,556±4000。获得了一种均一的AcPase I，并给出了其碳水化合物组成。