Some properties of purified phytohemagglutinin from Lens culinaris seeds

Abstract

Lens culinaris phytohemagglutinin was purified by specific adsorption on Sephadex G-100 and subsequent displacement with d-glucose. The homogeneity of the purified hemagglutinin was ascertained by ultracentrifugal analysis and polyacrylamide gel electrophoresis. The purified hemagglutinin had a s 0 20, w value of 3.4 S. This hemagglutinin was disclosed to be a kind of glycoprotein containing 1.5% glucose and 0.5% glucosamine. The specificity of the purified hemagglutinin was tested by hemagglutination-inhibition assays and found to be essentially the same as that of concanavalin A. In each step of the purification, the mitogenic activity against human peripheral lymphocytes was found to be always confined to the fraction which had the hemagglutinating activity. Morphological studies on hemagglutinin-stimulated cultures indicated that at 72 h about 15% of the cell population had been transformed by the purified hemagglutinin.