Abstract:
:We have studied the oligosaccharide chains of the variant surface glycoprotein (VSG) of Trypanosoma brucei brucei MITat 1.6. Glycopeptides were generated by Pronase digestion, purified by gel permeation and ion-exchange chromatography, and structurally characterized by 1H and 31P NMR spectroscopy in combination with chemical composition analyses. The two glycopeptide fractions obtained each proved to be homogeneous in their peptide and heterogeneous in their carbohydrate structures. The fraction representing the "internal" N-glycosylation site of the VSG was found to contain high-mannose type oligosaccharides with structures Man7-9GlcNAc2 linked to Asn-Ala-Thr. The other glycopeptide fraction contained the membrane-anchoring C-terminal glycan of the VSG attached to Asp. Its oligosaccharide structures are of the glycosylphosphatidylinositol (GPI) type: [structure: see text] This structure includes revisions of multiple structural features published for the GPI anchor of T. b. brucei MITat 1.6 VSG by Schmitz et al. (1987) Biochem. Biophys. Res. Commun. 146: 1055-1063.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Strang AM,Allen AK,Holder AA,van Halbeek Hdoi
10.1006/bbrc.1993.2412subject
Has Abstractpub_date
1993-11-15 00:00:00pages
1430-9issue
3eissn
0006-291Xissn
1090-2104pii
S0006291X83724125journal_volume
196pub_type
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