The immunological and physicochemical properties of mitogenic proteins derived from Phaseolus vulgaris.

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  • 1 May 1972
    • journal article
    • Vol. 22  (5) , 871-83
Abstract
A commercially available phytohaemagglutinin derived from Phaseolus vulgaris (PHAP) was subjected to CM Sephadex and Sephadex G-150 chromatography. Two major mitogenic fractions were isolated; one (L-PHAP), appeared homogeneous by polyacrylamide gel electrophoresis, and was virtually lacking in haemagglutinating activity, while the other (H-PHAP) was a potent haemagglutinin. H-PHAP was a complex material as shown by its behaviour on CM Sephadex chromatography. Electrophoretic analysis revealed three distinct bands of protein, all migrating cathodally to L-PHAP. With increasing cathodal mobility H-PHAP subfractions showed diminishing mitogenicity, increasing haemagglutinating potency, and the appearance of the ability to precipitate serum proteins non-specifically. The latter property, present in crude PHAP, was not displayed by L-PHAP. The mitogenic activity of all H-PHAP subfractions was potentiated by the presence of autologous red blood cells.