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 journalArticle

17 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1640-1647
Number of pages8
JournalJournal of Neurochemistry
Volume68
Issue number4
Publication statusPublished - Jan 1 1997
Externally publishedYes

    Fingerprint

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Chadli, A., LeCaer, J. P., Bladier, D., Joubert-Caron, R., & Caron, M. (1997). Purification and characterization of a human brain galectin-1 ligand. Journal of Neurochemistry, 68(4), 1640-1647.