Binding of N-linked bovine fetuin glycopeptides to isolated rabbit hepatocytes: Gal/GalNAc hepatic lectin discrimination between Gal beta(1,4)GlcNAc and Gal beta(1,3)GlcNAc in a triantennary structure.
Binding of N-linked bovine fetuin glycopeptides to isolated rabbit hepatocytes: Gal/GalNAc hepatic lectin discrimination between Gal beta(1,4)GlcNAc and Gal beta(1,3)GlcNAc in a triantennary structure.
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N-连接牛胎球蛋白糖肽与分离的兔肝细胞的结合:三触角结构中 Gal/GalNAc 肝凝集素区分 Gal beta(1,4)GlcNAc 和 Gal beta(1,3)GlcNAc。
DOI:
10.1021/bi00367a055
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发表时间:
1986
期刊:
影响因子:
2.9
通讯作者:
Lee,YC
中科院分区:
文献类型:
--
作者:
Townsend,RR;Hardy,MR;Wong,TC;Lee,YC
Department of Biology and McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218 Received March 7, 1986; Revised Manuscript Received May 14, 1986 abstract: Glycopeptides were isolated from bovine fetuin after digestion with Pronase, aminopeptidase M, and carboxypeptidase Y. Theglycopeptides were derivatized with tert-butyloxycarbonyltyrosine and separated on the basis of peptide by using reverse-phase high-performanceliquid chromatography. Using 400-MHz'H NMR, the asialotriantennary oligosaccharides at each of the three N-linked glycosylation sites were found to be combinations of the following two structures in which the third branch is either Gal (3 (l, 4) GlcNAc or Gal/3 (l, 3) GlcNAc: