The binding of d-glucosyl-neoglycoproteins to the hepatic asialoglycoprotein receptor.
The binding of d-glucosyl-neoglycoproteins to the hepatic asialoglycoprotein receptor.
复制标题
d-葡萄糖基新糖蛋白与肝脱唾液酸糖蛋白受体的结合。
DOI：
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发表时间：
1978
影响因子：
4.8
通讯作者：
Y. Lee
中科院分区：
文献类型：
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作者：
C. Stowell;Y. Lee
对D-葡萄糖基新糖蛋白和D-半乳糖末端糖蛋白与兔肝去唾液酸糖蛋白受体的结合进行了表征和比较。这两种类型的糖蛋白的结合表现出相同的依赖于钙浓度，神经氨酸酶的敏感性，和各种碳水化合物衍生物的抑制程度。这些结果，沿着观察到兔肝膜以相同程度结合D-葡萄糖基和D-半乳糖基封端的糖蛋白，表明两种类型的糖蛋白结合相同的受体。为了证实这一假设，受体分离从兔肝脏通过亲和层析使用D-半乳糖基-牛血清白蛋白或D-葡萄糖基-牛血清白蛋白固定在琼脂糖凝胶。这些受体被证明是相同的几个化学和免疫学标准，以及在他们的能力，结合等量的D-半乳糖基和D-葡萄糖基终止的糖蛋白。结论是兔肝去唾液酸糖蛋白受体不能区分D-半乳糖基和D-葡萄糖基终止的糖蛋白，并结合两者。
The binding of D-glucosyl-neoglycoproteins and D-galactose-terminated glycoproteins to the hepatic asialoglycoprotein receptor of rabbit liver membranes were characterized and compared. The binding of both types of glycoproteins showed the same dependence on calcium concentration, sensitivity to neuraminidase, and degree of inhibition by various carbohydrate derivatives. These results, along with the observation that the rabbit liver membranes bound both the D-glucosyl- and D-galactosyl-terminated glycoproteins to the same extent, indicated that both types of glycoproteins bound to the same receptor. To confirm this hypothesis, receptors were isolated from rabbit livers by affinity chromatography using D-galactosyl-bovine serum albumin or D-glucosyl-bovine serum albumin immobilized on Sepharose. These receptors were shown to be identical by several chemical and immunological criteria as well as in their ability to bind equal amounts of D-galactosyl- and D-glucosyl-terminated glycoproteins. The conclusion is that the rabbit hepatic asialoglycoprotein receptor cannot discriminate between D-galactosyl and D-glucosyl-terminated glycoproteins and binds both.