摘要
研究纤连蛋白受体（FnR）分子中N-糖链对其与纤连蛋白（Fn）结合的影响。利用纤连蛋白片断亲和层析柱和麦胚凝集素亲和层析柱，从人胎盘组织中纯化得到了FnR，经SDS-聚丙烯酞胺凝胶电泳证实为α和β两个亚基所组成。制备嵌合FnR的脂质体后，用糖甘酶处理以获得合不同糖链结构FnR脂质体，研究FnR分子中糖链在受体与配体结合中的作用。结果：用唾液酸酶处理嵌合FnR的脂质体，与Fn的粘附能力保持不变。嵌合FnR的脂质体单用p-N-乙酰氨基葡萄糖苷酶处理，或用唾液酶，β-N-乙酰氨基葡萄糖苷酶，β-半乳糖苷酶三者联合处理，其与Fn的粘附能力均下降50％。结论：FnR上糖链改变确实能影响FnR与Fn的结合，但FnR糖链上末端的唾液酸可能不影响两者的结合，而FnR糖链上末端或平分型N-乙酸氨基葡萄糖（GlcNAc）在两者结合时可能起重要作用。
PURPOSE To study the effect of N - oligosacchides of fibronectin receptor (FnR) on the binding of FnRto fibronetin (Fn).METHODS ① Purification of FnR from human placenta by the Fn fragment affinity column and WGAaffinity column. ② Dertemination the ability of Fn - containing liposome adhesion to Fn coated plates.RESULTS The ability of FnR containing liposome adhesion to Fn coated plates was not decreased aftertreatment of the lipome with sialidase, but decreased by 50 % after treatment of the liposome with β- N -acetyglucosaminidase, and also decreased by 50 % after treatment of liposome with sialidase, β- N - galactosi-dase, β- N - acetyglucosaminidase together.CONCLUSIONS N -glycan of FnR plays the biological role in the interaction between Fn and FnR, andN-acetylglucosarnine residue and (or) bisect - glucosamine on the FnR glycan is important during the interac-tion betwen FnR and Fn, but the sialic acid risidue on FnR glycan is not.
出处
《上海医科大学学报》
CSCD
1997年第5期331-334,共4页
Journal of Fudan University(Medical Science)
