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兔小肠刷状缘膜氨肽酶N的碳水化合物部分。

The carbohydrate moiety of aminopeptidase N of rabbit intestinal brush-border membrane.

作者信息

Massey D, Maroux S

出版信息

FEBS Lett. 1985 Feb 25;181(2):207-10. doi: 10.1016/0014-5793(85)80261-1.

Abstract

Endoglycosidase F was used to eliminate the N-linked complex glycans from intestinal aminopeptidase N. The glycans which were probably O-linked remaining after the endoglycosidase F treatment exhibited the human blood group A and H determinants expressed in enzymes from A+ or A- rabbits, respectively. The molecular mass estimation of the two types of glycans by SDS-polyacrylamide gel electrophoresis and the sugar composition of aminopeptidase from A+ and A- rabbits strongly suggested the presence of eight N-linked complex glycans and two O-linked oligosaccharides bearing the human group antigenicity.

摘要

使用内切糖苷酶F去除肠氨肽酶N上的N-连接复合聚糖。内切糖苷酶F处理后剩余的可能为O-连接的聚糖分别在来自A+或A-兔的酶中表现出人类血型A和H决定簇。通过SDS-聚丙烯酰胺凝胶电泳对两种聚糖进行分子量估计以及对A+和A-兔氨肽酶的糖组成分析强烈表明存在八个N-连接复合聚糖和两个具有人类血型抗原性的O-连接寡糖。

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