Attachment of thioglycosides to proteins: enhancement of liver membrane binding.

Attachment of thioglycosides to proteins: enhancement of liver membrane binding.
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硫代糖苷与蛋白质的结合:增强肝膜结合。

DOI:
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发表时间:
1976
期刊:
影响因子:
2.9
通讯作者:
Hans H. Liu
Hans H. Liu
中科院分区:
生物学3区
文献类型:
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作者:
M. Krantz;N. Holtzman;C. Stowell;Yuan C. Lee;Jerry W. Weiner;Hans H. Liu

文献摘要

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D-半乳糖、D-葡萄糖、N-乙酰基-D-葡萄糖胺和D-甘露糖的硫代糖苷通过脒化、重氮偶联和酰胺形成共价连接到米曲霉α-淀粉酶、鸡蛋溶菌酶和牛血清白蛋白。使用脱唾液酸类粘蛋白作为参考,测量新形成的糖蛋白(新糖蛋白)与兔肝膜的结合。通过这三种方法中的任何一种连接 D-半乳糖苷可将结合增强几个数量级。偶联相当数量的 D-甘露糖苷或 N-乙酰基-D-氨基葡萄糖苷几乎没有影响或没有影响。 D-葡萄糖苷的附着也增强了结合,但程度不同,具体取决于附着方法。因此,就糖特异性而言,新糖蛋白对兔肝膜的行为与血清糖蛋白的行为非常相似(Ashwell 和 Morell,1974)。
Thioglycosides of D-galactose, D-glucose, N-acetyl-D-glucosamine, and D-mannose were covalently attached to Aspergillus oryzae alpha-amylase, hen's eggs lysozyme, and bovine serum albumin by amidination, diazo coupling, and amide formation. The binding of the newly formed glycoproteins (neoglycoproteins) to rabbit liver membranes was measured, using asialoorosomucoid as a reference. Attachment of D-galactosides by any of the three methods enhanced binding by several orders of magnitude. Coupling of a comparable number of D-mannosides or N-acetyl-D-glucosaminides had little or no effect. Attachment of D-glucosides also enhanced binding but to a variable extent depending on the method of attachment. Thus, the behavior of neoglycoproteins toward rabbit liver membranes closely paralleled that of serum glycoproteins (Ashwell and Morell, 1974) with respect to sugar specificity.