INTERACTION OF BRAIN SPECTRIN (FODRIN) WITH PHOSPHOLIPIDS

被引：35

作者：

DIAKOWSKI, W ^{[1
]}

SIKORSKI, AF ^{[1
]}

机构：

[1] UNIV WROCLAW, INST BIOCHEM, PL-51148 WROCLAW, POLAND

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 40期

关键词：

D O I：

10.1021/bi00040a041

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：

Binding of brain spectrin to frozen and thawed liposomes was studied, using a pelleting assay, as a function of Lipid composition. Saturable binding was observed for all lipid mixtures that included aminophospholipids, as well as for the total lipid of synaptic plasma membranes. Binding was strong and saturable, with dissociation constants in the nanomolar range. There were two pH optima at ca. 6.0 and 7.5 and a sharp ionic strength optimum, corresponding to physiological solvent conditions. No competition could be detected with extraneous globular proteins, serum albumin, and hemoglobin. The results imply a strong, direct interaction between brain spectrin and the neuronal plasma membrane in the cell.

引用

页码：13252 / 13258

页数：7

共 48 条

[31] ANKYRIN BINDING TO (NA+ + K+)ATPASE AND IMPLICATIONS FOR THE ORGANIZATION OF MEMBRANE DOMAINS IN POLARIZED CELLS [J].