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. 1969 Aug;63(4):1439–1446. doi: 10.1073/pnas.63.4.1439

SOLUBILIZATION AND PARTIAL CHARACTERIZATION OF A PHYTOHEMAGGLUTININ RECEPTOR SITE FROM HUMAN ERYTHROCYTES

Stuart Kornfeld 1, Rosalind Kornfeld 1
PMCID: PMC223484  PMID: 5261914

Abstract

Trypsin treatment of human erythrocytes releases a soluble glycopeptide which binds to phytohemagglutinin and abolishes the erythroagglutinating and lymphocyte-stimulating properties of this molecule. The glycopeptide has been purified by alkaline borohydride treatment, proteolytic digestion, gel filtration, and DEAE-cellulose chromatography. The most highly purified glycopeptide has a molecular weight of about 2,000. The specificity for binding to phytohemagglutinin resides in the oligosaccharide portion of the molecule with the determinant sugar being a galactose residue which is penultimate to a N-acetylneuraminic acid in some chains and uncovered in others. The glycopeptide is about 3,000 times more potent than either N-acetylgalactosamine or galactose in inhibiting the mitogenic response of lymphocytes induced by phytohemagglutinin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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