Interaction of lectins with their ligand carbohydrate of alpha-fetoprotein: analysis by mixed-lectin affinity electrophoresis.
Serum or ascites alpha-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 allo 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.
Taketa
K
K
Department of Public Health, Okayama University Medical School, Japan.
Liu
M
M
Taga
H
H
D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D006528:Carcinoma, Hepatocellular / Q000097:blood / Q000378:metabolism; D003208:Concanavalin A; D004587:Electrophoresis, Agar Gel; D015180:Electrophoresis, Gel, Two-Dimensional; D005312:Fetal Blood / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D008024:Ligands; D008969:Molecular Sequence Data; D010835:Phytohemagglutinins / Q000378:metabolism*; D037121:Plant Lectins; D000509:alpha-Fetoproteins / Q000378:metabolism*
C045794:Allomyrina lectin; D037102:Lectins; D008024:Ligands; D010835:Phytohemagglutinins; D037121:Plant Lectins; D000509:alpha-Fetoproteins; C067494:erythroagglutinating phytohemagglutinin; C033619:lentil lectin; D003208:Concanavalin A