PURIFICATION OF MITOGENIC PROTEINS FROM HURA-CREPITANS AND ROBINIA-PSEUDACCACIA

The lectin-mitogens from H. crepitans and R. pseudacaccia were purified by affinity chromatography and compared to that from A. precatorius by sodium lauryl sulfate gel electrophoresis. Robinia lectin is quite similar to that from A. precatorius in that it consists of 2 distinct polypeptide chains of 32,000 and 30,000 daltons, but unlike Abrus lectin the chains are not joined by disulfide bonds. Hura lectin is composed of a single polypeptide chain which migrates identically with the H chain of the Abrus lectin. This H chain is likely to be responsible for binding to galactose residues on cell surfaces. The lectin from R. pseudaccacia was obtained in crystalline form.