PROTEOLIPIDS .V. ACTIVITY OF LIPID CYTOCHROME C

被引：22

作者：

SUN, FF

CRANE, FL

机构：

[1] Department of Biological Sciences, Purdue University Lafayette

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1969年 / 172卷 / 03期

关键词：

D O I：

10.1016/0005-2728(69)90138-8

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：

Lipid-cytochrome c prepared according to the procedure of Das and Crane1 was found to be highly active in the transfer of electrons from ascorbate via tetramethyl-p-phenylenediamine and the cytochrome oxidase system to O2. The proteolipid can be assayed in aqueous medium after microdispersion by sonication. An assay method is described in detail. Lipid-cytochrome c micelles aggregate at or below pH 5.5, and the aggregate has no detectable activity. The pH optimum of lipid-cytochrome c oxidation was found at pH 6.0. High ionic strength which decomposes the lipid complex also impairs the activity. These observations are discussed in terms of the phospholipid requirements of the cytochrome-oxidase reaction. © 1969.

引用

页码：417 / &

共 23 条

[1]

BARTLETT GR, 1959, J BIOL CHEM, V234, P466

[2] STUDIES OF ELECTRON-TRANSFER SYSTEM .48. PHOSPHOLIPID REQUIREMENTS IN CYTOCHROME OXIDASE [J].