Premium
Interaction of lectins with their ligand carbohydrate of α‐fetoprotein: Analysis by mixed‐lectin affinity electrophoresis
Author(s) -
Taketa Kazuhisa,
Liu Miao,
Taga Hiroko
Publication year - 1996
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150170309
Subject(s) - lectin , affinity electrophoresis , concanavalin a , soybean agglutinin , chemistry , biochemistry , electrophoresis , agarose , microbiology and biotechnology , agglutinin , peanut agglutinin , wheat germ agglutinin , affinity chromatography , biology , enzyme , in vitro
Serum or ascites α‐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.