Author/Authors :
Vasily D. Antonenkov، نويسنده , , Paul P. Van Veldhoven، نويسنده , , Etienne Waelkens، نويسنده , , Guy P. Mannaerts، نويسنده ,
Title Of Article :
Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver
Latin Abstract :
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 KCl by dissociating into monomers with poor activity, thiolase A retained its full activity and its homodimeric structure under these conditions
NaturalLanguageKeyword :
thiolase , L-Oxidation , Clo¢brate , peroxisome , (Rat liver)
JournalTitle :
Studia Iranica
