An improved method for purification of wheat germ agglutinin (lectin) by affinity chromatography

Abstract

A simple purification of wheat germ agglutinin from commercial wheat germ is described. From defatted ground wheat germ, the lectin was extracted and then purified in a single step by filtration on an ion exchange chromatography column and adsorption on an insolubilized N-acetyl glucosamine derivative. The amount of lectin obtained from 1,000 g of wheat germ was larger than 500 mg. Although the yield was at least twice higher than that obtained with other methods, no impurities could be detected, and molecular characteristics are in good agreement with the protein purified by more sophisticated procedures.