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
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.
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页码:731 / 734
页数:4
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