Interaction of lectins with their ligand carbohydrate of α-fetoprotein: Analysis by mixed-lectin affinity electrophoresis

✍ Scribed by Professor Kazuhisa Taketa; Miao Liu; Hiroko Taga

• Publisher: John Wiley and Sons
• Year: 1996
• Tongue: English
• Weight: 450 KB
• Volume: 17
• Category: Article
• ISSN: 0173-0835
• DOI: 10.1002/elps.1150170309

✦ Synopsis

Interaction of lectins with their ligand carbohydrate of a-fetoprotein: Analysis by mixed-lectin affinity electrophoresis

Serum or ascites a-fetoprotein (AFP) from patients with hepatocellular carcinoma and from a cord blood were analyzed by affinity electrophoresis with two lectins mixed in agarose gel in a combination of concanavalin A (Con A) and Lens culinaris agglutinin A (LCA-A) or of erythroagglutinating phytohemagglutinin (E-PHA) and Allomyrina dichotoma lectin (allo A). Con A-and LCA-A-reactive AFP-C2-L3 was not further retarded by mixing with either of the other lectin. It showed a mobility identical with that of AFP-C2 or AFP-L3. E-PHA-and all0 A-reactive AFP-P4-A3 showed similar results. It migrated with intermediate mobilities of AFP-P4 and AFP-A3 depending on the concentrations of the two lectins mixed in the gel. The results indicate that the two mixed lectins compete with each other for the topologically different lectin-binding sites on the oligosaccharide of AFP molecule.