微钙蛋白酶对肝脏网蛋白的蛋白水解作用。

Proteolysis of liver plectin by mu-calpain.

作者信息

Muenchbach M, Dell'Ambrogio M, Gazzotti P

机构信息

Laboratory of Biochemistry III, Swiss Federal Institute of Technology (ETH), Zurich, CH-8092, Switzerland.

出版信息

Biochem Biophys Res Commun. 1998 Aug 19;249(2):304-6. doi: 10.1006/bbrc.1998.9138.

DOI:10.1006/bbrc.1998.9138

PMID:9712691

Abstract

Rat liver plectin was found to be mainly associated with plasma membrane fractions enriched in junctional complexes. The membrane-associated plectin has been partially isolated. Plectin co-purifies with a 200 kDa polypeptide which, on the basis of sequence homology, has been identified as a myosin like-protein. The interaction of mu-calpain with liver plectin has been investigated. Plectin is very sensitive to mu-calpain and is digested to give a fragment of 240 kDa.

摘要

研究发现大鼠肝脏的网蛋白主要与富含连接复合体的质膜组分相关。已部分分离出与膜相关的网蛋白。网蛋白与一种200 kDa的多肽共同纯化，基于序列同源性，该多肽被鉴定为一种肌球蛋白样蛋白。已对μ-钙蛋白酶与肝脏网蛋白的相互作用进行了研究。网蛋白对μ-钙蛋白酶非常敏感，会被消化产生一个240 kDa的片段。