钙调蛋白与磷脂的相互作用。

Interaction of caldesmon with phospholipids.

作者信息

Czuryło E A, Zborowski J, Dabrowska R

机构信息

Department of Muscle Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.

出版信息

Biochem J. 1993 Apr 15;291 ( Pt 2)(Pt 2):403-8. doi: 10.1042/bj2910403.

DOI:10.1042/bj2910403

PMID:8484721

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1132539/

Abstract

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 (Kass. = 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.

摘要

已通过色氨酸荧光光谱法研究了钙调蛋白与由各种磷脂组成的脂质体之间的相互作用。结果表明，钙调蛋白与磷脂酰丝氨酸（PS）囊泡形成的复合物最强（结合常数Kass = 1.45×10⁵ M⁻¹）。静电相互作用和疏水相互作用都有助于该复合物的稳定性。PS的强结合位点似乎位于钙调蛋白34 kDa C端片段的N端部分。PS在该位点的结合导致钙调蛋白从其与钙调蛋白的复合物中被置换出来。