Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver

被引：24

作者：

Antonenkov, VD ^{[1
]}

Van Veldhoven, PP ^{[1
]}

Waelkens, E ^{[1
]}

Mannaerts, GP ^{[1
]}

机构：

[1] Katholieke Univ Leuven, Dept Mol Celbiol, B-3000 Louvain, Belgium

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1999年 / 1437卷 / 02期

关键词：

peroxisome; thiolase; beta-oxidation; clofibrate; (rat liver);

D O I：

10.1016/S1388-1981(99)00003-7

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 specific activities and substrate specificities of 3-oxoacyl-CoA thiolase A (thiolase A) purified from normal rat liver peroxisomes and 3-oxoacyl-CoA thiolase B (thiolase B) isolated from livers of rats treated with the peroxisome proliferator clofibrate were virtually identical. The enzymes could be distinguished by their N-terminal amino acid sequences, their isoelectric points and their stability, the latter being higher for thiolase A. Contrary to thiolase B, which showed a marked cold lability in the presence of KCI by dissociating into monomers with Door activity, thiolase A retained its full activity and its homodimeric structure under these conditions. (C) 1999 Elsevier Science B,V. All rights reserved.

引用

页码：136 / 141

页数：6

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