Abstract
Summary Cytosol from pig blood platelets catalysed the transfer of phosphatidylinositol from liposomes to mitochondria or from microsomes to liposomes. Gel filtration on Sephadex G 100 allowed to isolate two fractions displaying apparent molecular weights of 29 000 and 18 000, which were purified 4 and 6.4 fold, respectively. Neither crude cytosol nor the purified fractions stimulated the transfer of phosphatidic acid, from liposomes to mitochondria or from red cell ghost to liposomes, suggesting that the purified proteins are strongly specific for phosphatidylinositol. The lack of phosphatidic acid exchange proteins in platelet cytosol is discussed in relation to recent findings concerning the phosphatidylinositol cycle in stimulated platelets.
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