IDENTIFICATION OF ALTERED SUBUNIT IN INACTIVE F1-ATPASE OF AN ESCHERICHIA-COLI-UNCA MUTANT

被引：45

作者：

DUNN, SD

机构：

[1] Section of Biochemistry, Molecular and Cell Biology Cornell University, Ithaca

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1978年 / 82卷 / 02期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

D O I：

10.1016/0006-291X(78)90916-6

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：

ATPase activity was restored to the inactive coupling factor, F1ATPase, of Escherichia coli strain AN120 (uncA401) by reconstitution of the dissociated complex with an excess of wild-type α subunit. Large excesses of α gave the highest levels of activity. The other subunits which are required for the reconstitution of ATPase activity, β and γ, did not complement the mutant enzyme. These results indicate that the α polypeptide of the AN120 ATPase is defective. © 1978.

引用

页码：596 / 602

页数：7

共 20 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] PURIFICATION AND CHARACTERIZATION OF INACTIVE CA-2+,MG-2+-ACTIVATED ADENOSINE-TRIPHOSPHATASE OF UNC A-MUTANT ESCHERICHIA-COLI AN120 [J].