Activation of phosphorylating vesicles by net transfer of phosphatidyl choline by phospholipid transfer protein |
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Authors: | Y Kagawa L W Johnson E Racker |
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Affiliation: | 1. Section of Biochemistry & Molecular Biology Cornell University, Ithaca, New York 14850 USA;2. the Graduate School of Nutrition Cornell University, Ithaca, New York 14850 USA |
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Abstract: | Vesicles formed with phosphatidyl ethanolamine, phosphatidyl choline, cardiolipin, coupling factors and hydrophobic proteins from bovine heart mitochondria catalyzed a rapid32Pi-ATP exchange. When phosphatidyl choline was deleted during the assembly of the vesicles, little32Pi-ATP exchange was observed. Exchange activity was induced by incubating such deficient vesicles with phosphatidyl choline liposomes in the presence of a phosphatidyl choline transfer protein isolated from bovine heart. Transfer of [32P] phosphatidyl choline was demonstrated by isolation of the activated vesicles by sucrose density centrifugation. |
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Keywords: | PC phosphatidyl choline PE phosphatidyl ethanolamine coupling factor 1 (ATPase) OSCP oligomycin sensitivity-conferring protein |
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