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 language | English (US) |
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Pages (from-to) | 1640-1647 |
Number of pages | 8 |
Journal | Journal of Neurochemistry |
Volume | 68 |
Issue number | 4 |
DOIs | |
State | Published - Apr 1997 |
Externally published | Yes |
Keywords
- Affinity chromatography
- Central nervous system
- Galectin
- Heat shock protein
- Human brain
- Lectin
ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience