Purification of a phosphatidylinositol/phosphatidylcholine transfer protein from Neurospora crassa.
This paper reports, for the first time, the purification of a phospholipid transfer protein (PLTP) from a fungus, Neurospora crassa. The protein was purified from the post-microsomal supernatant of N. crassa by successive chromatography on DEAE-cellulose, Sephadex-G75 and PBE 94 (pH 4-7). The purified protein (M(r) 38,000) was found to transfer phosphatidylinositol preferentially over phosphatidylcholine, like the PLTP from the yeast, Saccharomyces cerevisiae. PC transfer was completely inhibited by inactivation of free amino groups or tryptophan residues. Surprisingly, the protein did not cross-react with antibodies against the bovine brain PITP. The cellular content of the protein was maximal during the logarithmic phase of growth. However, no direct correlation between the content of the protein and PC transfer activity could be demonstrated.
Basu
J
J
Department of Chemistry, Bose Institute, Calcutta, India.
Kundu
M
M
Chakrabarti
P
P
D000727:Androgen-Binding Protein; D015153:Blotting, Western; D002352:Carrier Proteins / Q000302:isolation & purification*; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins; D009492:Neurospora crassa / Q000737:chemistry*; D010713:Phosphatidylcholines; D010716:Phosphatidylinositols; D049294:Phospholipid Transfer Proteins; D029701:Saccharomyces cerevisiae Proteins
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; D008565:Membrane Proteins; D010713:Phosphatidylcholines; D010716:Phosphatidylinositols; D049294:Phospholipid Transfer Proteins; C118289:SEC24 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins