WISTARIA-SINENSIS AGGLUTININ - PURIFICATION, CARBOHYDRATE SPECIFICITY, AND CHARACTERIZATION OF THE COMBINING SITE
WISTARIA-SINENSIS AGGLUTININ - PURIFICATION, CARBOHYDRATE SPECIFICITY, AND CHARACTERIZATION OF THE COMBINING SITE
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DOI：
10.1016/0008-6215(88)85051-1
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发表时间：
1988-06-15
影响因子：
3.1
通讯作者：
CHATTERJEE, BP
中科院分区：
文献类型：
--
作者：
AHMED, H;CHATTERJEE, BP
用2-乙酰氨基-2-脱氧-D-半乳糖-淀粉偶联物亲和层析法从紫云英种子中纯化出一种2-乙酰氨基-2-脱氧-D-半乳糖结合凝集素，聚丙烯酰胺圆盘凝胶电泳结果表明该凝集素是均一的。它有一个摩尔。重量66，000（Sephadex G-150凝胶过滤）;在2-巯基乙醇存在下的SDS-聚丙烯酰胺凝胶电泳上，它解离成mol.重量34，000，表明凝集素是二聚体;它是一种糖蛋白，含有4.8%的碳水化合物。它凝集几种脊椎动物的红细胞，包括人类，无论血型如何。在半抗原抑制试验中，发现2-乙酰氨基-2-脱氧-D-半乳糖及其糖苷是比D-半乳糖及其糖苷更好的抑制剂，但N-乙酰基-乳糖胺是最有效的抑制剂。半抗原的HO-3，4和HO-2部分参与结合。
A 2-acetamido-2-deoxy-D-galactose-binding agglutinin from Wistaria sinensis seeds, purified by affinity chromatography on a 2-acetamido-2-deoxy-D-galactose-starch conjugate, was homogeneous as judged by poly(acrylamide) disc gel electrophoresis. It had a mol. wt. of 66,000 (gel filtration on Sephadex G-150); on electrophoresis on SDS-poly(acrylamide) gel in the presence of 2-mercaptoethanol, it dissociated into sub-units of mol. wt. 34,000, suggesting the agglutinin to be a dimer; and it was a glycoprotein containing 4.8% of carbohydrate. It agglutinated several vertebrate erythrocytes, including human regardless of the blood group. In hapten-inhibition assays, 2-acetamido-2-deoxy-D-galactose and its glycosides were found to be better inhibitors than D-galactose and its glycosides, but N-acetyl-lactosamine was the most potent inhibitor. The binding involved HO-3,4 of the haptens and HO-2 partially.