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

共 5 条

[1] PURIFICATION AND IMMUNOLOCALIZATION OF THE PEROXISOMAL 3-OXOACYL-COA THIOLASE FROM SACCHAROMYCES-CEREVISIAE
ERDMANN, R
KUNAU, WH
YEAST, 1994, 10 (09) : 1173 - 1182
[2] Localization of peroxisomal 3-oxoacyl-CoA thiolase in particles of varied density in rat liver: Implications for peroxisome biogenesis
vanRoermund, CWT
vandenBerg, M
Wanders, RJA
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS, 1995, 1245 (03): : 348 - 358
[3] ZONAL DISTRIBUTION OF PEROXISOMAL 3-OXOACYL-COA THIOLASE MESSENGER-RNA IN LIVER FROM RATS TREATED WITH DI-(2-ETHYLHEXYL)PHTHALATE
BOUT, A
DEBOER, PAJ
TAGER, JM
BENNE, R
MOORMAN, AFM
BIOCHIMICA ET BIOPHYSICA ACTA, 1990, 1055 (03) : 240 - 242
[4] Substrate specificity of THCA-CoA oxidases from rat liver light mitochondrial fractions on dehydrogenation of 3α,7α,12α-trihydroxy-5β-cholestanoic acid CoA thioester
Ikegawa, S
Goto, T
Mano, N
Goto, J
STEROIDS, 1998, 63 (11) : 603 - 607
[5] Further characterization of the peroxisomal 3-hydroxyacyl-CoA dehydrogenases from rat liver - Relationship between the different dehydrogenases and evidence that fatty acids and the C-27 bile acids di- and tri-hydroxycoprostanic acids are metabolized by separate multifunctional proteins
DieuaideNoubhani, M
Novikov, D
Baumgart, E
Vanhooren, JCT
Fransen, M
Goethals, M
Vandekerckhove, J
VanVeldhoven, PP
Mannaerts, GP
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 240 (03): : 660 - 666

← 1 →