Lipid dependence of glucose-6-phosphate phosphohydrolase: a study with purified phospholipid transfer proteins and phosphatidylinositol-specific phospholipase C.
Lipid dependence of glucose-6-phosphate phosphohydrolase: a study with purified phospholipid transfer proteins and phosphatidylinositol-specific phospholipase C.
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DOI:
10.1021/bi00521a035
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发表时间:
1981-09
期刊:
影响因子:
2.9
通讯作者:
R. Crain;D. B. Zilversmit
中科院分区:
文献类型:
--
作者:
R. Crain;D. B. Zilversmit
Richard C. Crain1 and Donald B. Zilversmit*· 5 abstract: The nonspecific and phosphatidylcholine-specific transfer proteins from beef liver and the phosphatidylinositol-specific phospholipase C from Staphylococcus aureus were used to modify the phospholipid composition of micro-somal membranes in order to study the dependence of glu-cose-6-phosphate phosphohydrolase (EC 3.1. 3.9) activity on membrane phospholipids. Incubation of microsomes with dipalmitoylphosphatidylcholine-containing unilamellar vesicles and either transfer protein produced a membrane in which this disaturated phospholipid contributed up to 43% of the total phosphatidylcholine. Incubation of microsomes and phos-phatidylcholine unilamellar vesicles with nonspecific transfer protein caused a net increase in the membrane phosphatidylcholine content and a net decrease in the phosphatidylethanolamine and phosphatidylinositol levels, whereas in incubations with the phosphatidylcholine transfer protein, no change in phospholipid class composition occurred. Incubations of microsomes and phosphatidylcholine/phosphatidylethanolamine (3: 1 mol/mol) unilamellar vesicles with the nonspecific transfer protein alsocaused an increased phos-phatidylcholine content and a decreased phosphatidylinositolINíumerous membrane-bound enzymes have been found to have a functional dependence on the lipid bilayer (Sander-mann, 1978). This was clearly demonstrated by Fleischer and co-workers (1962) who first showed a role of phospholipids in the mitochondrial electron transfer system by (a) removing