STABILIZATION OF AN ACETYL-COENZYME A CARBOXYLASE COMPLEX FROM PSEUDOMONAS-CITRONELLOLIS

被引：17

作者：

FALL, RR ^{[1
]}

机构：

[1] UNIV COLORADO, DEPT CHEM, BOULDER, CO 80309 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1976年 / 450卷 / 03期

关键词：

D O I：

10.1016/0005-2760(76)90022-9

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：

Using stabilizing conditions, the acetyl-CoA carboxylase (EC 6.4.1.2) of P. citronellolis was isolated as a complex containing 4 different polypeptide chains with MW of 53,000, 36,000, 33,000 and 25,000. These polypeptide chains probably corresponded to distinct biotin carboxylase, transcarboxylase and biotin carboxyl carrier protein subunits in analogy with similar subunits of Escherichia coli acetyl-CoA carboxylase, an unstable complex in vitro.

引用

页码：475 / 480

页数：6

共 10 条

[1]

Alberts A.W., 1972, ENZYMES, V6, P37, DOI 10.1016/S1874-6047(08)60037-2

[2] ANALYSIS OF BACTERIAL BIOTIN-PROTEINS [J].