RELATIONSHIP BETWEEN LIPID SATURATION AND LIPID PROTEIN-INTERACTION IN LIVER-MITOCHONDRIA MODIFIED BY CATALYTIC-HYDROGENATION WITH REFERENCE TO CARDIOLIPIN MOLECULAR-SPECIES

被引:65
作者
SCHLAME, M
HORVATH, L
VIGH, L
机构
[1] HUMBOLDT UNIV BERLIN,CHARITE HOSP,INST PATHOL & CLIN BIOCHEM,O-1086 BERLIN,GERMANY
[2] BIOL RES CTR,INST BIOPHYS,H-6701 SZEGED,HUNGARY
关键词
D O I
10.1042/bj2650079
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 acyl double bonds in isolated mitochondrial membranes were gradually reduced by palladium-complex-catalysed hydrogenation, and the resulting saturation was monitored by fatty acid analysis of phospholipids suggested that cardiolipin is in a membrane compartment which is less accessible to the applied catalyst. Native cardiolipin and its hydrogenation products were further characterized by analysis of their molecular diacylglycerol species. A decrease in the double bond content was accompanied by an increased amount of motionally restricted lipids at the hydrophobic interface of proteins as measured by two different spin-labelled lipids (C-14 positional isomers of spin-labelled stearic acid and phosphatidylcholine analogues). The protein-immobilized fraction of spin-labelled stearic acid increased in parallel with the hydrogenation of cardiolipin rather than of phosphatidylcholine or phosphatidylethanolamine. These data are interpreted in terms of a tight association of cardiolipin with membrane proteins, which becomes looser upon double bond reduction leading to the replacement of cardiolipin by spin-labelled stearic acid in the solvation shell. Thus the hydrophobic moiety of cardiolipin, characterized by double-unsaturated C18-C18 diacylglycerol species, seems to be an important structural requirement for the high protein affinity of this compound.
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页码:79 / 85
页数:7
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