Basu J, Kundu M, Bhattacharya U, Mazumder C, Chakrabarti P
Department of Chemistry, Bose Institute, Calcutta, India.
Biochim Biophys Acta. 1988 Mar 25;959(2):134-42. doi: 10.1016/0005-2760(88)90024-0.
A non-specific lipid transfer protein has been purified from the pH 5.1 supernatant of goat liver by DEAE-cellulose, CM-cellulose and Sephadex G-75 column chromatography. The protein shows a single band on polyacrylamide gel electrophoresis and transfers 450 nmol of phosphatidylcholine per min per mg of protein under the present assay condition. This protein has a subunit molecular weight of 12,000 and an isoelectric point of 8.65. Amino acid analysis reveals the absence of methionine. Histidine has been identified as the only N-terminal amino acid. Besides phosphatidylcholine, the protein transfers phosphatidylinositol, phosphatidylethanolamine, phosphatidylserine and cholesterol. Chemical modification studies showed the involvement of free amino and thiol groups in the maintenance of the transfer activity of the goat liver protein.
一种非特异性脂质转移蛋白已通过DEAE-纤维素、CM-纤维素和葡聚糖凝胶G-75柱色谱法从山羊肝脏pH 5.1的上清液中纯化出来。该蛋白在聚丙烯酰胺凝胶电泳上显示出一条单一的条带，并且在当前的测定条件下，每毫克蛋白每分钟转移450纳摩尔的磷脂酰胆碱。这种蛋白的亚基分子量为12000，等电点为8.65。氨基酸分析表明不存在甲硫氨酸。已鉴定出组氨酸是唯一的N端氨基酸。除了磷脂酰胆碱外，该蛋白还转移磷脂酰肌醇、磷脂酰乙醇胺、磷脂酰丝氨酸和胆固醇。化学修饰研究表明，游离氨基和巯基参与维持山羊肝脏蛋白的转移活性。
