Structural characterization of the asparagine-linked oligosaccharides from Trypanosoma brucei type II and type III variant surface glycoproteins.
作者： S.E. Zamze , D.A. Ashford , E.W. Wooten , T.W. Rademacher , R.A. Dwek
DOI: 10.1016/S0021-9258(18)54916-4
关键词: C-terminus 、 Biochemistry 、 Galactose 、 Asparagine 、 Glycoprotein 、 Endoglycosidase 、 Stereochemistry 、 Trypanosoma brucei 、 Oligosaccharide 、 Biology 、 Glycosylation
摘要: The complete primary structures of the major Asn-linked oligosaccharides from type II variant surface glycoproteins (VSGs), MITat 1.2 and 1.7, III VSG, 1.5, were determined using a combination exo- endoglycosidase digestions, methylation analysis, acetolysis, 500 MHz 1H NMR spectroscopy. Each contained classical branched oligomannose-type biantennary complex oligosaccharides, proportion latter substituted with terminal alpha(1-3)-linked galactose residues, first report presence this epitope in Trypanosoma brucei. In addition both variants relatively large amounts unusual small Man4GlcNAc2 Man3GlcNAc2, diverse array novel poly-N-acetyllactosamine similar but not identical to those mammalian glycoproteins. These also partially residues. Glycosylation showed site specificity that Man(9-5)GlcNAc2 located exclusively at Asn-glycosylation 1 very close C terminus, whereas Man(4-3)GlcNAc2 2. This is protozoa.
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