CONCURRENT IDENTIFICATION OF CALPAIN-I AND CALPAIN-II FROM CHICKEN SKELETAL-MUSCLE

被引：9

作者：

BIRKHOLD, SG ^{[1
]}

SAMS, AR ^{[1
]}

机构：

[1] TEXAS A&M UNIV,DEPT POULTRY SCI,COLLEGE STN,TX 77843

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1994年 / 107卷 / 04期

关键词：

CALPAIN; SKELETAL MUSCLE;

D O I：

10.1016/0305-0491(94)90179-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A single anion-exchange column resolved two peaks of calcium-activated neutral protease activity, corresponding to the two calpain forms from chicken skeletal muscle. Multiple columns have previously been needed to resolve the two isoforms from avian tissue. Calcium requirement assays confirmed one form to require approximately 100 mu M Ca2+ for half-maximal activity, while the other required approximately 500 mu M Ca2+. Electrophoresis revealed that the enzymes were not purified to homogeneity.

引用

页码：519 / 523

页数：5

共 15 条

[1] CALCIUM-ACTIVATED NEUTRAL PROTEASE (CALPAIN) SYSTEM - STRUCTURE, FUNCTION, AND REGULATION [J].