Isolation of glycopeptides containing individual glycosylation sites of Friend murine leukemia virus glycoprotein: studies of glycosylation by methylation analysis.
Glycopeptides containing individual N-glycosylation sites of the glycoprotein from Friend murine leukemia virus were isolated by digestion of the viral glycoprotein with protease of S. aureus (V8) or with trypsin followed by fractionation of the resulting (glyco)peptides by gel filtration and reversed-phase, high-performance liquid chromatography at pH 6. Isolated glycopeptides were assigned to the known amino acid sequence of the protein by amino acid analysis and by determination of the NH2-termini. The carbohydrate moieties of each glycosylation site were analysed by methylation analysis. A high selectivity of the glycoprotein glycosylation was found with regard to the distribution of oligomannosidic, mixed, and N-acetyl-lactosaminic oligosaccharides.
D000818:Animals; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002460:Cell Line; D010450:Endopeptidases; D005622:Friend murine leukemia virus / Q000032:analysis*; D006020:Glycopeptides / Q000302:isolation & purification*; D006023:Glycoproteins / Q000302:isolation & purification*; D008745:Methylation; D051379:Mice; D012697:Serine Endopeptidases; D014357:Trypsin; D014764:Viral Proteins / Q000302:isolation & purification*
D006020:Glycopeptides; D006023:Glycoproteins; D014764:Viral Proteins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin