猪心脏微粒体中膜结合型CD38/ADP-核糖基环化酶的差异寡聚化

Differential oligomerization of membrane-bound CD38/ADP-ribosyl cyclase in porcine heart microsomes.

作者信息

Chidambaram N, Wong E T, Chang C F

机构信息

Department of Biochemistry, Faculty of Medicine, National University of Singapore, Singapore.

出版信息

Biochem Mol Biol Int. 1998 May;44(6):1225-33. doi: 10.1080/15216549800202322.

DOI:10.1080/15216549800202322

PMID:9623778

Abstract

A protein fraction displaying ADP-ribosyl cyclase activity was purified from porcine heart microsomes which appeared as a major band of 45 kDa on Coomassie blue stained SDS-PAGE gel under reducing condition. Protein immunoblot analysis with antiserum to recombinant rat CD38 showed a series of bands (45-285 kDa) under nonreducing condition, while only the 45 kDa monomer under reducing condition. The high molecular weight oligomers of CD38 were found to be stable even upon treatment with various concentrations of SDS in the sample buffer and also upon incubation at lower temperature. These oligomers of CD38 also displayed higher ADP-ribosyl cyclase activity than that of the monomer.

摘要

从猪心脏微粒体中纯化出一种具有ADP - 核糖基环化酶活性的蛋白质组分，在还原条件下，考马斯亮蓝染色的SDS - PAGE凝胶上它呈现为一条45 kDa的主要条带。用抗重组大鼠CD38抗血清进行蛋白质免疫印迹分析，在非还原条件下显示出一系列条带（45 - 285 kDa），而在还原条件下仅显示45 kDa的单体。发现即使在样品缓冲液中用各种浓度的SDS处理以及在较低温度下孵育，CD38的高分子量寡聚体也很稳定。这些CD38寡聚体的ADP - 核糖基环化酶活性也高于单体。