Coppens I, Bastin P, Courtoy P J, Baudhuin P, Opperdoes F R
Cell Biology Unit, University of Louvain Medical School, Brussels, Belgium.
Biochem Biophys Res Commun. 1991 Jul 15;178(1):185-91. doi: 10.1016/0006-291x(91)91797-g.
The trypanosome LDL receptor has been isolated from bloodstream form and cultured insect-stage trypanosomes as a protein of Mr 145,000, using a rapid purification procedure in the presence of a cocktail of protease inhibitors, whereas previously a polypeptide of Mr 86,000 was purified as the LDL receptor. Both the 145,000 and the 86,000 polypeptides are glycosylated and recognized by a monospecific antibody raised against the 86,000 species. This antibody inhibits LDL binding to the intact trypanosomes, to the isolated 145,000 receptor and to the 86,000 species. Hence, the previously isolated 86,000 polypeptide is a degradation product probably representing the cleaved-off ectodomain of the trypanosome LDL receptor.
已利用一种在蛋白酶抑制剂混合物存在下的快速纯化程序,从血液型锥虫和培养的昆虫阶段锥虫中分离出分子量为145,000的锥虫低密度脂蛋白(LDL)受体蛋白,而之前纯化的LDL受体是一种分子量为86,000的多肽。145,000和86,000的这两种多肽均被糖基化,并可被针对86,000分子量物种产生的单特异性抗体识别。该抗体可抑制LDL与完整锥虫、分离出的145,000受体以及86,000分子量物种的结合。因此,之前分离出的86,000多肽是一种降解产物,可能代表锥虫LDL受体被切割掉的胞外结构域。