| pubmed-article:7742351 | pubmed:abstractText | 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 19,000, 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 high 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 degrees C and optimal pH 4-7. Heating protein at 100 degrees C does not inactivate protein whereas a denaturation with urea is irreversible. | lld:pubmed |
