EFFECTS OF DIFFERENT ENZYMATIC TREATMENTS ON THE RELEASE OF TITIN FRAGMENTS FROM RABBIT SKELETAL MYOFIBRILS - PURIFICATION OF AN 800 KDA TITIN POLYPEPTIDE

被引：23

作者：

ASTIER, C ^{[1
]}

LABBE, JP ^{[1
]}

ROUSTAN, C ^{[1
]}

BENYAMIN, Y ^{[1
]}

机构：

[1] UNIV MONTPELLIER 1,EPHE,MOTIL CELLULAIRE LAB,CTR RECH BIOCHIM MACROMOLEC,CNRS,LP 9008,F-34060 MONTPELLIER,FRANCE

来源：

BIOCHEMICAL JOURNAL | 1993年 / 290卷

关键词：

D O I：

10.1042/bj2900731

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：

In myofibrils, titin (also called connectin) molecules span from Z line to M line and constitute a third filament system containing an elastic domain in the I band. This giant protein is particularly sensitive to proteolysis in situ. Treatment of rabbit skeletal myofibrils with exogenous proteinases induces a release of titin fragments, which are detected in the soluble myofibrillar fraction. The cleavage of titin occurs at specific points localized at the proximity of Z Iine and could lead to a concomitant release of alpha-actinin.

引用

页码：731 / 734

页数：4

共 30 条

[1]

ASTIER C, 1991, COMP BIOCH PHYSL B, V100, P465

[2] THE ORGANIZATION OF TITIN FILAMENTS IN THE HALF-SARCOMERE REVEALED BY MONOCLONAL-ANTIBODIES IN IMMUNOELECTRON MICROSCOPY - A MAP OF 10 NONREPETITIVE EPITOPES STARTING AT THE Z-LINE EXTENDS CLOSE TO THE M-LINE [J].