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Purification and Characterization of a Human Brain Galectin‐1 Ligand
Author(s) -
Chadli Ahmed,
LeCaer JeanPierre,
Bladier Dominique,
JoubertCaron Raymonde,
Caron Michel
Publication year - 1997
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1997.68041640.x
Subject(s) - human brain , galectin , chemistry , molecular mass , ligand (biochemistry) , peptide , affinity chromatography , lectin , biochemistry , mass spectrometry , heat shock protein , chromatography , biology , enzyme , receptor , neuroscience , gene
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.