Abstract
A novel phospholipid transfer protein has been purified to homogeneity 406-fold from the filamentous fungus Aspergillus oryzae. The successive steps of purification comprised ultrafiltration, gel filtration on Sephadex G-75, ion exchange chromatographies on DEAE-Sepharose and Mono Q. The active protein is a monomer with a molecular mass of 19000, estimated from SDS electrophoresis, amino acid composition as well, as gel filtration. The isoelectric point is 4.8. The amino acid composition is characterized by a hight amount of Gly, Leu, Ser, Asx and Glx residues and 4 Cys residues. N-terminal sequence was determined and compared with M. mucedo sequence. The purified protein was found to transfer preferentially phosphatidylglycerol and phosphatidylinositol over phosphatidylcholine > phosphatidylethanolamine > phosphatidylserine and no phosphatidic acid. Optimal temperature for in vitro transfer was 25–30° C and optimal pH 4–7. Heating protein at 100° C does not inactivate protein whereas a denaturation with urea is irreversible.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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