Isolation and Characterization of Concanavalin A from the seeds of Canavalia ensiformis

Abstract

Concanavalin A was isolated from Jackbean (Canavalia ensiformis) seeds. The protein was purified by using affinity chromatography. The activity of the Con A was determined by haemagglutinin assay and the purity of the protein was tested by Sodium dodecyl sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). The activity of lectins is quantified by their ability to agglutinate erythrocyte. The eluted protein exhibited agglutinating activity when reacted against different types of fresh erythrocytes. In SDS-PAGE, it has been concluded that the molecular weight of Concanavalin A is 104 kDa. It is a homotetramer in which transition metals (Magnesium or Calcium ions) are bound to each subunit that helps this lectin to bind to α-mannose or α-galactose in sugars