The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins.
The isolation and properties of a rabbit liver binding protein specific for asialoglycoproteins.
复制标题
脱唾液酸糖蛋白特异性兔肝结合蛋白的分离和特性。
DOI：
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发表时间：
1974
影响因子：
4.8
通讯作者：
A. Morell
中科院分区：
文献类型：
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作者：
R. L. Hudgin;W. Pricer;G. Ashwell;R. Stockert;A. Morell
摘要 早期报道了肝质膜结合去唾液酸糖蛋白作为运输和分解代谢前奏的能力。本研究描述了通过亲和层析纯化肝蛋白，该肝蛋白保留了与膜相关的特征结合特性。分离出的物质是水溶性且不含脂质的，已被鉴定为一种糖蛋白，其中干重的 10% 由摩尔比为 1:1:2:2 的唾液酸、半乳糖、甘露糖和葡萄糖胺组成。末端唾液酸残基的完整性和钙的存在被证明是结合的绝对要求。物理化学研究表明最终的水溶性制剂中存在高度聚集。
Abstract The ability of hepatic plasma membranes to bind desialylated glycoproteins as a prelude to transport and catabolism has been reported earlier. The present study describes the purification, by affinity chromatography, of an hepatic protein which retains the characteristic binding properties associated with the membranes. The isolated material, which is watersoluble and free from lipids, has been identified as a glycoprotein in which 10 % of the dry weight consists of sialic acid, galactose, mannose, and glucosamine in a molar ratio of 1:1:2:2. The integrity of the terminal sialic acid residues and the presence of calcium were shown to be absolute requirements for binding. Physical chemical studies indicated a high degree of aggregation in the final, water-soluble preparation.