Basu J, Kundu M, Chakrabarti P
Department of Chemistry, Bose Institute, Calcutta, India.
Biochim Biophys Acta. 1992 Jun 26;1126(3):286-90. doi: 10.1016/0005-2760(92)90242-n.
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.
本文首次报道了从真菌粗糙脉孢菌中纯化磷脂转移蛋白（PLTP）。该蛋白通过在DEAE - 纤维素、葡聚糖G - 75和PBE 94（pH 4 - 7）上连续层析，从粗糙脉孢菌的微粒体后上清液中纯化得到。发现纯化后的蛋白（相对分子质量38,000）与来自酿酒酵母的PLTP一样，优先转移磷脂酰肌醇而非磷脂酰胆碱。游离氨基或色氨酸残基失活会完全抑制磷脂酰胆碱的转移。令人惊讶的是，该蛋白与抗牛脑PITP的抗体不发生交叉反应。该蛋白的细胞含量在生长对数期最高。然而，无法证明该蛋白的含量与磷脂酰胆碱转移活性之间存在直接关联。
