Purification and characterization of a human brain galectin-1 ligand

J Neurochem. 1997 Apr;68(4):1640-7. doi: 10.1046/j.1471-4159.1997.68041640.x.

Abstract

Our previous studies have characterized an endogenous lectin from human brain identified as galectin-1. A soluble ligand of galectin-1 was purified from human brain by affinity chromatography and preparative electrophoresis. The purified ligand (termed HBGp82, for human brain galectin-1-binding polypeptide of 82,000 daltons) has an apparent molecular mass of 82 kDa and is glycosylated by N-linked biantennary complex structures. HBGp82 was partially characterized by microsequencing of peptide fragments. Similar peptides were found in a heat shock of protein of 90,000 daltons, hsp90. However, comparison of apparent molecular weights and matrix-assisted laser desorption mass spectrometry clearly showed that HBGp82 differs to some degree from hsp90.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Brain Chemistry*
  • Chromatography, High Pressure Liquid
  • Galectin 1
  • Glycosylation
  • Hemagglutinins / analysis*
  • Hemagglutinins / isolation & purification
  • Hemagglutinins / metabolism
  • Humans
  • Lectins / analysis
  • Lectins / isolation & purification
  • Lectins / metabolism
  • Ligands
  • Mass Spectrometry
  • Molecular Sequence Data
  • Molecular Weight
  • Neuropeptides / analysis
  • Neuropeptides / isolation & purification
  • Neuropeptides / metabolism

Substances

  • Galectin 1
  • Hemagglutinins
  • Lectins
  • Ligands
  • Neuropeptides