Identification of the glycosylated sequons of human myelin-associated glycoprotein

Biochem Biophys Res Commun. 1993 Dec 15;197(2):457-64. doi: 10.1006/bbrc.1993.2501.

Abstract

Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope. MAG is heavily glycosylated containing 30% carbohydrate by weight. In this study, human MAG glycopeptides were isolated and sequenced. Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106. Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated. Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Asparagine
  • Cell Adhesion Molecules, Neuronal / chemistry
  • Cell Adhesion Molecules, Neuronal / metabolism
  • Chromatography, Affinity
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Glycopeptides / chemistry
  • Glycopeptides / isolation & purification
  • Glycosylation
  • Humans
  • Molecular Sequence Data
  • Myelin Proteins / chemistry*
  • Myelin Proteins / isolation & purification
  • Myelin Proteins / metabolism
  • Myelin-Associated Glycoprotein

Substances

  • Cell Adhesion Molecules, Neuronal
  • Glycopeptides
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • Asparagine