BINDING OF DEOXYCHOLATE TO LIPOPROTEIN-LIPASE

被引：25

作者：

BENGTSSON, G

OLIVECRONA, T

机构：

[1] Department of Chemistry, Section on Physiological Chemistry, University of Umeå

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 575卷 / 03期

关键词：

(Bovine milk); Deoxycholate binding; Lipoprotein lipase;

D O I：

10.1016/0005-2760(79)90118-8

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 deoxycholate to lipoprotein lipase from bovine milk was demonstrated by equilibrium dialysis and by charge shift electrophoresis. The detergent increased the solubility and stability of the enzyme in aqueous buffers, but did not change its elution position on gel filtration. It is concluded that each molecule of enzyme binds several molecules of deoxycholate without denaturation. This signifies the presence of a lipid-binding region in the native structure of the enzyme. © 1979.

引用

页码：471 / 474

页数：4

共 16 条

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EGELRUD, T
OLIVECRONA, T
[J]. BIOCHIMICA ET BIOPHYSICA ACTA, 1975, 381 (02) : 233 - 241

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