Purification of all thirteen polypeptides of bovine heart cytochrome c oxidase from one aliquot of enzyme Characterization of bovine fetal heart cytochrome c oxidase

FEBS Letters

Takamiya, Shinzaburo¹  Capaldi, Roderick A.¹  Lindorfer, Margaret A.¹ 

[1] Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA

关键词: Cytochrome-c oxidase;    Purification;    N-terminal sequence;    Subunit sequence;    Polypeptide separation;   

DOI  :  10.1016/0014-5793(87)81061-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A protocol has been worked out for separating all thirteen different polypeptides in the beef heart cytochrome c oxidase complex from a single aliquot of enzyme. This involves an initial separation of polypeptides by gel filtration on a Biogel P-60 column in SDS, a step which purifies subunits C_IV and C_VIII and gives mixtures of C_V+C_VI, ASA, AED and STA, as well as C_VII, C_IX and IHQ. These mixtures are then resolved by reverse-phase high-performance liquid chromatography. The separation procedures have been applied to fetal heart cytochrome c oxidase of gestation between 100 and 200 days. No differences were found in the N-terminal sequences of any of the cytoplasmically made subunits or in the entire sequence of C_IX between late fetal and adult forms of the enzyme.

【 授权许可】

Unknown