The glycoprotein 71 of ecotropic Friend murine leukemia virus. Structure of the oligosaccharides linked to asparagine-12

FEBS Lett. 1984 Apr 24;169(2):194-8. doi: 10.1016/0014-5793(84)80317-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Asparagine / analysis*
  • Carbohydrate Sequence
  • Endopeptidases / metabolism
  • Friend murine leukemia virus / analysis*
  • Gas Chromatography-Mass Spectrometry
  • Glycoproteins / analysis*
  • Neuraminidase / metabolism
  • Oligosaccharides / analysis*
  • Serine Endopeptidases*

Substances

  • Glycoproteins
  • Oligosaccharides
  • Asparagine
  • Neuraminidase
  • Endopeptidases
  • Serine Endopeptidases
  • glutamyl endopeptidase