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- W78369080 abstract "This chapter provides an overview of the interaction of lectins with human lymphocytes. The lymphocyte surface bears receptors that are related to the function and differentiation of these cells. The receptors for lectins consist of the carbohydrate chains of glycoproteins and possibly also glycolipids exposed on the external cell membrane. In an experiment described in the chapter, the receptors were studied by a surface-labeling technique. Lymphocytes contain several glycoproteins. Several of these glycoproteins act as receptors for the Ricinus communis agglutinin, concanavalin A, kidney bean leucoagglutinin, wheat germ, and soybean agglutinins. Of these lectins, concavalin A and leucoagglutinin are strongly lymphocyte-stimulating, while the Ricinus communis agglutinin inhibits DNA synthesis. The wheat germ and soybean agglutinins are neither toxic nor stimulating for normal lymphocytes. Several major membrane glycoproteins contain receptors for lymphocyte-stimulaing and nonstimulating lectins. In transforming lymphocytes, the external glycoprotein pattern changes and a protein that is strongly labeled without galactose oxidase treatment appears." @default.
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- W78369080 date "1976-01-01" @default.
- W78369080 modified "2023-09-23" @default.
- W78369080 title "Interaction of lectins with human lymphocytes studied by a surface-labeling technique" @default.
- W78369080 doi "https://doi.org/10.1016/b978-0-12-233750-5.50017-8" @default.
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