MITOCHONDRIAL ATPASE COMPLEX OF ASPERGILLUS-NIDULANS AND THE DICYCLOHEXYLCARBODIIMIDE-BINDING PROTEIN

被引：32

作者：

TURNER, G

IMAM, G

KUNTZEL, H

机构：

[1] Department of Bacteriology, University of Bristol Medical School, University Walk, Bristol

[2] Faculty of Science, Mansura University, Mansura

[3] Abteilung Chemie, Max-Planck-Institut Fur Experimentelle Medizin, Göttingen, D-3400

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 97卷 / 02期

关键词：

D O I：

10.1111/j.1432-1033.1979.tb13145.x

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 dicyclohexylcarbodiimide‐binding protein of Aspergillus nidulans has been identified as the smallest subunit of the mitochondrial ATPase complex, and has a molecular weight of approximately 8000. It is extractable from whole mitochondria and from the purified enzyme in neutral chloroform/methanol, contains 30% polar amino acids, and the N‐terminal amino acid has been identified as tyrosine. Using a double‐labelling technique in the absence and presence of cycloheximide, followed by immunoprecipitation of the enzyme complex with antiserum against Neurospora crassa F1 ATPase, it has been shown that this subunit is synthesized on cytoplasmic ribosomes. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：565 / 571

页数：7

共 33 条

[1] CIRCULAR DNA FROM MITOCHONDRIA OF NEUROSPORA-CRASSA [J].