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对腹足纲软体动物罗曼蜗牛Helix pomatia的氧运输蛋白(βC-血清蛋白)的功能单位e中的碳水化合物进行了研究.以该βC-血清蛋白为载体,通过限制性胰蛋白酶水解,产生片段a-c,ef,以及功能单位d,g,和h.以片段ef降解后的产物为研究对象,通过亲合色谱的分离纯化,得到功能单位e的一个馏分e2.该馏分经还原、吡啶乙基化和胰蛋白酶水解后,通过柱色谱的分离纯化,得到一个含有糖肽的成分.对该糖肽中糖组分和肽序列的分析,最终确定了功能单位e的两个糖基化位置:Asn-111和Asn-387.通过与功能单位d和g的糖基化位置的比较得出结论:Asn-387为一恒定的糖基化位置.“,”The carbohydrate in functional unit e of βC-haemocyanin of the gastropod Helix pomatia was studied. The limited trypsinolysis on tenth molecules of βC-haemocyanin of Helix pomatia at pH = 8. 2 yielded the fragments αc, e f, and the functional units d, g, and h (present as dimers h2). The mixture of functional units e and f after limited fragmentation of fragment ef on storage, were further fractionated with an affinity chromatography in the presence of α-methylglucoside, yielded functional unit e2. Further separation of trypsinolysis of pyridylethylated functional unit e2 yielded a fraction I (contain glycopeptides). The analysis of carbohydrate content and the N-terminal sequence allowed the location of the carbohydrate and the identification of the glycosylation sites in functional unit e: site A at Asn-111 and site B at Asn-387. From a comparison with the glycosylation sites of Hp d and Hp g, it follows that the site B is a conserved one.