The glycoprotein 71 of ecotropic Friend murine leukemia virus. Structure of the oligosaccharides linked to asparagine-12.
The glycoprotein from Friend murine leukemia virus was digested with protease from Staphylococcus aureus V8. A glycopeptide comprising the N-terminal glycosylation site (Asn-12) was isolated from the mixture of fragments and analyzed by amino acid sequencing and methylation-capillary gas chromatography-mass spectrometry before and after treatment with sialidase from Vibrio cholerae. Asn-12 was thus found to be substituted by a family of partially sialylated, fucosylated, and intersected glycoprotein N-glycans of the hybrid type.
D000595:Amino Acid Sequence; D001216:Asparagine / Q000032:analysis*; D002240:Carbohydrate Sequence; D010450:Endopeptidases / Q000378:metabolism; D005622:Friend murine leukemia virus / Q000032:analysis*; D008401:Gas Chromatography-Mass Spectrometry; D006023:Glycoproteins / Q000032:analysis*; D009439:Neuraminidase / Q000378:metabolism; D009844:Oligosaccharides / Q000032:analysis*; D012697:Serine Endopeptidases
D006023:Glycoproteins; D009844:Oligosaccharides; D001216:Asparagine; D009439:Neuraminidase; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase