Isolation and characterization of lectins from red seeds of Abrus precatorius

Abstract

The study was done to isolate lectin from red seeds of Abrus precatorius. The protein was purified by using affinity chromatography. The activity of the lectin 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 in affinity 2 bands were observed of 34kD and 31kD of heterotetrameric agglutinin.