PURIFICATION AND CHARACTERIZATION OF CITRATE SYNTHASE ISOENZYMES FROM PSEUDOMONAS-AERUGINOSA

被引：17

作者：

MITCHELL, CG ^{[1
]}

ANDERSON, SCK ^{[1
]}

ELMANSI, EMT ^{[1
]}

机构：

[1] UNIV BATH,DEPT BIOCHEM,BATH BA2 7AY,AVON,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1995年 / 309卷

关键词：

D O I：

10.1042/bj3090507

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：

Two types of citrate synthase (CS) have been purified from Pseudomonas aeruginosa, a 'large' form (CSI) and a 'small' form (CSII). The M(r)s of the CSI and CSII isoenzymes were determined to be 240000+/-16000 (mean+/-S.E.M.) and 80300+/-3800 respectively. Chemical cross-linking of the native enzymes with either dimethyl suberimidate or glutaraldehyde followed by electrophoretic analysis by SDS/PAGE showed that CSI is a hexamer and CSII is a dimer. SDS/PAGE showed that CSI and CSII each consist of a single subunit type, of M(r) 42000+/-2000 and M(r) 36 500+/-2000 respectively. CSI and CSII were also shown to be distinct kinetically, immunologically and in terms of their regulatory properties. It is suggested that the CS isoenzymes are products of different structural genes.

引用

页码：507 / 511

页数：5

共 39 条

[21] FREEZING OF DCMP AMINOHYDROLASE IN ACTIVATED CONFORMATION BY GLUTARALDEHYDE [J].