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.
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| Evidence ID | Analyze ID | Gene/Complex | Systematic Name/Complex Accession | Qualifier | Gene Ontology Term ID | Gene Ontology Term | Aspect | Annotation Extension | Evidence | Method | Source | Assigned On | Reference |
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| Evidence ID | Analyze ID | Regulator | Regulator Systematic Name | Target | Target Systematic Name | Direction | Regulation of | Happens During | Regulator Type | Direction | Regulation Of | Happens During | Method | Evidence | Strain Background | Reference |
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| Complement ID | Locus ID | Gene | Species | Gene ID | Strain background | Direction | Details | Source | Reference |
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| Evidence ID | Analyze ID | Dataset | Description | Keywords | Number of Conditions | Reference |
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