INTERACTION OF CALDESMON WITH PHOSPHOLIPIDS

被引：12

作者：

CZURYLO, EA

ZBOROWSKI, J

DABROWSKA, R

机构：

[1] M NENCKI INST EXPTL BIOL,DEPT MUSCLE BIOCHEM,3 PASTEUR ST,PL-02093 WARSAW,POLAND

[2] M NENCKI INST EXPTL BIOL,DEPT CELLULAR BIOCHEM,PL-02093 WARSAW,POLAND

来源：

BIOCHEMICAL JOURNAL | 1993年 / 291卷

关键词：

D O I：

10.1042/bj2910403

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：

The interaction of caldesmon with liposomes composed of various phospholipids has been examined by tryptophan fluorescence spectroscopy. The results indicate that caldesmon makes its strongest complex with phosphatidylserine (PS) vesicles (K(ass) = 1.45 x 10(5) M-1). Both electrostatic and hydrophobic interactions contribute to the stability of this complex. The site for strong binding of PS seems to be located in the N-terminal part of the 34 kDa C-terminal fragment of caldesmon. Binding of PS at this site results in displacement of calmodulin from its complex with caldesmon.

引用

页码：403 / 408

页数：6

共 40 条

[1] MYOSIN LIGHT CHAIN AND CALDESMON PHOSPHORYLATION IN ARTERIAL MUSCLE STIMULATED WITH ENDOTHELIN-1 [J].