PROTEIN-DETERGENT INTERACTIONS STUDIED BY CAPILLARY ISOTACHOPHORESIS

被引：11

作者：

HJALMARSSON, SG

机构：

[1] LKB-Produkter AB, Research Department

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 581卷 / 02期

关键词：

Bovine serum albumin; Detergent-protein interaction; Isotachophoresis; Ovalbumin;

D O I：

10.1016/0005-2795(79)90240-X

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 interactions of sodium dodecyl sulphate with bovine serum albumin and ovalbumin have been studied by capillary isotachophoresis. This method makes it possible to determine very accurately the number of ligands bound to the high-affinity binding sites of the native protein. Bovine serum albumin was found to have seven high-affinity binding sites whereas ovalbumin in its native state was found to lack high-affinity binding sites for dodecyl sulphate. © 1979.

引用

页码：210 / 216

页数：7

共 15 条

[1]

CLARKE S, 1975, J BIOL CHEM, V250, P5459

[2]

DELMOTTE P, 1978, ELECTROPHORESIS, V78, P115

[3]

GILLBERG.G, 1970, BIOCHEM BIOPH RES CO, V38, P137

[4] SOLUBILIZATION OF MEMBRANES BY DETERGENTS [J].