Purification and characterization of a human brain galectin-1 ligand

Ahmed Chadli, Jean Pierre LeCaer, Dominique Bladier, Raymonde Joubert-Caron, Michel Caron

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1640-1647
Number of pages8
JournalJournal of Neurochemistry
Issue number4
StatePublished - Apr 1997
Externally publishedYes


  • Affinity chromatography
  • Central nervous system
  • Galectin
  • Heat shock protein
  • Human brain
  • Lectin

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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