【摘要】 分离纯化了人胎盘纤连蛋白（Ｆｎ），经ＳＤＳ－ＰＡＧＥ鉴定为一条带，纯化Ｆｎ仍保持其搞原性，得率为３８．７％。根据植物凝集素识别专一糖链结构的原理，应用斑点印迹法，亲和层析法和Ｗｅｓｔｅｒｎ转移电泳研究糖链结构，结果证实：１．人胎盘Ｆｎ分子中含有复杂型Ｎ糖链（包括二天线和大于二天线的结构）以及高甘露糖型和／或杂合型Ｎ糖链；复杂型Ｎ糖链中含有平分型ＧｌｃＮＡｃ，糖链末端也可连有唾液酸；２．胰糜蛋白酶水解而获得的明胶结合片段（４４ｋＤ）含有二天线和多天线复杂型糖链，也可接有平分型ＧｌｃＮＡｃ；３．肝素结合片段（３０ｋＤ）以及明胶、肝素均不结合的Ｆｎ片段不含有多天线复杂型Ｎ糖链。更多还原

【Abstract】 Fibronectin (Fn) is a glycoprotein with high molecular weight and consists of a number of domains. The analyses of structure of oligosaccharide linked to the domains is useful to elucidate the role of oligosaccharide in the function of certain domain. Human placenta Fn was purified with 38.7% recovery. It appears as one single band on SDS-PAGE and still maintains its antigenicity. In terms of the principle of recognition of the lectin to the oligosaccharides specifically, dot blot, affinity chromatography and Western bolt electrophoresis were applied to analyse the structure of oligosaccharides. The results suggested that 1. Human placenta Fn contains complex type (including bi-, tri- and tetraantenery), high mannose type and/or hybrid type of N-linked oligosaccharides; complex types of N-linked oligosaccharides contain bisecting GlcNAc and sialic acid at terminal;2.gelatin-binding fragment (44kD) obtained by chymotrypsinization have complex type of N-linked Oligosaccarides with the bisecting GlcNAc, including bi-, Tri- and tetra antenery;3. both heparin-binding fragments (30kD) and gelatin、heparin-nonbound fragments do not have complex type of N-oligosaccharide.更多还原