The role of residual phospholipids and copurified proteins in the reconstitution of bovine heart mitochondrial ATPase complex.

Abstract:

:The reactivation of mitochondrial ATPase by acidic and isoelectric phospholipids was studied comparatively with two purified enzyme preparations exhibiting different gel electrophoretic patterns: the preparation of Serrano et al. (1976, J. Biol. Chem. 251, 2453-2461) and the complex V of Galante et al. (1979, J. Biol. Chem. 254, 12372-12379). Isoelectric phosphatidylcholine liposomes showed marked differences in affinity for the two ATPase complexes and produced different maximal reactivations, whereas no significant differences were found with negatively charged liposomes. Analysis of residual phospholipids associated with the two ATPase preparations revealed a greater relative cardiolipin content in complex V. It is proposed that the different patterns of reactivation of the two ATPase preparations by isoelectric phospholipids result from different contents in residual cardiolipin and adenine nucleotide carrier.

authors

Dabbeni-Sala F,Palatini P

doi

10.1016/0006-291x(85)90976-3

subject

Has Abstract

pub_date

1985-12-17 00:00:00

pages

807-13

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)90976-3

journal_volume

133

pub_type

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