DIVALENT METALS OF MYELIN AND THEIR DIFFERENTIAL BINDING BY MYELIN BASIC-PROTEIN OF BOVINE CENTRAL-NERVOUS-SYSTEM

被引：32

作者：

BERLET, HH

BISCHOFF, H

WEINHARDT, F

机构：

[1] Institute of Pathochemistry and General Neurochemistry, University of Heidelberg, D-69120 Heidelberg

来源：

NEUROSCIENCE LETTERS | 1994年 / 179卷 / 1-2期

关键词：

BOVINE SPINAL CORD; MYELIN; MYELIN BASIC PROTEIN; TRACE METAL; ZINC; MAGNESIUM; METAL BINDING;

D O I：

10.1016/0304-3940(94)90938-5

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

Divalent metal ions are being implicated in the compaction of myelin. Levels of Cd, Co, Cu, Hg, Mn, Pb, Zn, Ca and Mg of isolated myelin of bovine central nervous system (CNS) were measured by flame atomic absorption spectrophotometry. Binding of these metal ions by isolated myelin basic protein (MBP, Mr 18,500) of bovine CNS was concurrently assessed by centrifugal equilibrium dialysis. Metals were bound in the order of Hg > Cu > Zn > Mg > Cd > Co, exempting Mn, Pb and Ca. The results are indicative of differential metal affinity of MBP which may account for the immobilization or anchoring of MBP in myelin by zinc and other divalent metal cations.

引用

页码：75 / 78

页数：4

共 27 条

[1] METAL-AFFINITY SEPARATIONS - A NEW DIMENSION IN PROTEIN PROCESSING [J].