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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Dabbeni-Sala F,Palatini Pdoi
10.1016/0006-291x(85)90976-3subject
Has Abstractpub_date
1985-12-17 00:00:00pages
807-13issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(85)90976-3journal_volume
133pub_type
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journal_title:Biochemical and biophysical research communications
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journal_title:Biochemical and biophysical research communications
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