NOVEL GLYCOSYLATION ROUTES FOR GLYCOPROTEINS - THE LACDINAC PATHWAY
NOVEL GLYCOSYLATION ROUTES FOR GLYCOPROTEINS - THE LACDINAC PATHWAY
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DOI:
10.1042/bst0230175
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发表时间:
1995-02-01
影响因子:
3.9
通讯作者:
VANDIE, I
中科院分区:
文献类型:
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作者:
VANDENEIJNDEN, DH;NEELEMAN, AP;VANDIE, I
Protein-and lipid-linked complex-type oligosaccharide chains are commonly based on GalPl-+ 4GlcNAc (N-acetyl-lactosamine, lacNAc) units that serve as backbone structural elements. However, in an increasing number of instances GalNAca 1-+ 4GlcNAc (4”-diacetyl-lactosdiamine, 1acdiNAc) units rather than lacNAc units are found on the N-and 0-linked oligosaccharide chains of glycoproteins ([l-241; see Table 1). The group of glycoproteins that carry such chains is quite diverse and comprises inter alia hormones, enzymes, membrane glycoproteins and transport proteins. It appears that lacdiNAc-type chains particularly occur on glycoproteins of lower animal species, but are also present along with lacNAc-type chains on mammalian glycoproteins. Like the lacNAc unit in complex-type oligosaccharide structures, lacdiNAc units may be capped by terminal NeuAc residues in a2-3-or a2-6-linkage [S-121. They also may contain a Fuc residue in a 1-+ Slinkage to GlcNAc