Schmitz B, Klein R A
Biochem Biophys Res Commun. 1986 Dec 30;141(3):1274-8. doi: 10.1016/s0006-291x(86)80183-8.
The variant specific surface glycoprotein from Trypanosoma brucei brucei is incorporated into lipid vesicles using 8M urea as an unfolding reagent. Pronase treatment of these proteoliposomes removes most of the protein, leaving a glycophospholipopeptide which is the membrane attachment site. We show here that lectins, specific for mannose and galactose are able to recognize oligosaccharide residues on these proteoliposomes, using a straightforward aggregation assay. The relevance of these results obtained with the liposome model system to the accessibility of the surface antigens in living trypanosomes is discussed.
使用8M尿素作为展开剂，将布氏布氏锥虫的变体特异性表面糖蛋白整合到脂质囊泡中。用链霉蛋白酶处理这些蛋白脂质体可去除大部分蛋白质，留下作为膜附着位点的糖磷脂肽。我们在此表明，通过简单的聚集试验，对甘露糖和半乳糖具有特异性的凝集素能够识别这些蛋白脂质体上的寡糖残基。讨论了在脂质体模型系统中获得的这些结果与活锥虫中表面抗原可及性的相关性。
