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1969•The Journal of ImmunologyRequires access

Protein-Carbohydrate Interaction

Irwin Goldstein, Lucy L. So, Yvonne W.-H. Yang, Quinton Callies

Open publisher page 59 citations

Abstract

Abstract The specific interaction of concanavalin A, the phytohemagglutinin of the jack bean (Canavalia ensiformis), with several glycoproteins has been studied. It is demonstrated that concanavalin A forms precipitates with purified monoclonal IgM and the glycoprotein phytohemagglutinins (lectins) from waxbean and soybean. It is suggested that the carbohydrate residues reactive with concanavalin A are situated on the surface of these glycoproteins.

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What this paper is about

Abstract The specific interaction of concanavalin A, the phytohemagglutinin of the jack bean (Canavalia ensiformis), with several glycoproteins has been studied. It is demonstrated that concanavalin A forms precipitates with purified monoclonal IgM and the glycoprotein phytohemagglutinins (lectins) from waxbean and soybean. It is suggested that the carbohydrate residues reactive with concanavalin A are situated on the surface of these glycoproteins.

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Available abstract

Abstract The specific interaction of concanavalin A, the phytohemagglutinin of the jack bean (Canavalia ensiformis), with several glycoproteins has been studied. It is demonstrated that concanavalin A forms precipitates with purified monoclonal IgM and the glycoprotein phytohemagglutinins (lectins) from waxbean and soybean. It is suggested that the carbohydrate residues reactive with concanavalin A are situated on the surface of these glycoproteins.

Key concepts: Canavalia ensiformis, Concanavalin A, Glycoprotein, Lectin, Carbohydrate, Biochemistry, Monoclonal antibody, Chemistry

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