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Updated: Jul 30, 2026

A Lectin HPLC Method to Enrich Selectively-glycosylated Peptides from Complex Biological Samples
Published on: October 1, 2009
Purification and characterization of two lectins from a toxic moray, Gymnothrax javanicus
1Department of Applied Biological Chemistry, Faculty of Agriculture, Shizuoka University, Japan. achkawa@agr.shizuoka.ac.jp
Abstract:
Two lectins, Gymnothrax javanicus lectin-I (GJL-I) and Gymnothrax javanicus lectin-II (GJL-II) were isolated from the stomach and intestine, and the liver, respectively, of a toxic moray eel, Gymnothrax javanicus. GJL-I is a polymer of two heterogeneous subunits of 67 and 51 kDa. In a hemagglutination inhibition assay, it had sugar-binding specificity toward lactose and lactulose among the mono- or oligo-saccharides and bovine submaxillary mucin (BSM) among the glycoproteins tested. The lectin stimulated nerve growth factor (NGF) synthesis by astroglial cells. GJL-II was a polymer of subunit of 41 kDa. This lectin had N-acetyllactosamine binding specificity.
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