Abstract
A non-specific lipid transfer protein has been purified from a pH 5.1 supernatnat of germinated castor bean endosperms by column chromatographies on DEAE-Sepharose CL-6B, CM-Sepharose CL-6B, Sephadex G-50 and hydroxyapatite, when determined by the transfer of [ 14C]phosphatidylcholine from liposomes to mitochondria. The protein purified to homogeneity by polyacrylamide gel electrophoresis transferred 66 nmol phosphatidylcholine per min per mg of protein under the present assay condition. In addition to phosphatidylcholine transport, this protein transferred phosphatidylinositol, phosphatidylethanolamine, phosphatidylglycerol, phosphatidic acid, monogalactosyldiacylglycerol and digalactosyldiacylglycerol, but not diacylglycerol and triacylglycerol. The protein was a monomer with a molecular weight of about 9000, as estimated by molecular filtration through Sephadex G-50 and by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulphate. The amino acid analysis of this protein revealed a high amount of alanine and the absence of methionine, tyrosine and histidine. It gave an isoelectric point of higher than 10.5 as determined by isoelectric focusing.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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