Purification and characterization of Canavalia gladiata agglutinin.

A lectin from Japanese jack bean (Canavalia gladiata agglutinin, CGA) was purified by affinity chromatography on a maltamyl-Sepharose column. On sodium dodecyl sulfate-poly(acrylamide) gel electrophoresis, CGA was shown to have a protein subunit with a mol. wt. of 30,000. CGA has an amino acid composition similar to that of Concanavalin A. The lectin activity of CGA could be detected not only by hemagglutination assay with trypsinized human erythrocytes but also by the binding assay with intact horseradish peroxidase. The binding method could determine CGA in a concentration ranging from 50 to 500 ng/mL. The quantitative-inhibition studies of the binding indicated that CGA has sugar-binding specificities similar to those of concanavalin A.