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Immunology. May 1972; 22(5): 871–883.
PMCID: PMC1407857

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

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.

While L- and H-PHAP were closely related by immunological criteria, distinct differences were noted by three methods of analysis. The most cathodal of the H-PHAP subfractions was found to be immunodeficient by comparison with crude PHAP, L-PHAP, and the remaining H-PHAP subfractions. The implications of these findings with respect to the biological activity of PHAP and to its subunit structure are discussed.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Allen LW, Svenson RH, Yachnin S. Purification of mitogenic proteins derived from Phaseolus vulgaris: isolation of potent and weak phytohemagglutinins possessing mitogenic activity. Proc Natl Acad Sci U S A. 1969 Jun;63(2):334–341. [PMC free article] [PubMed]
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