Lectin Interactions with Normal and Tumor Cells and the Affinity Purification of Tumor Cell Glycoproteins

Nicolson, Garth L.

doi:10.1007/978-1-4612-6117-9_15

Garth L. Nicolson³

Part of the book series: Contemporary Biomedicine ((CB,volume 1))

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1 Citations

Abstract

Lectins, saccharide-binding proteins and glycoproteins which bind mono-or oligosaccharides specifically through their complementary sugar-binding sites, have been isolated from a wide variety of plants and animals (reviewed in Lis and Sharon, 1973; Nicolson, 1974a; Sharon and Lis, 1975; Roth, 1978; Goldstein and Hayes, 1978). Lectin interactions with carbohydrate-containing molecules on cells resemble antibody-antigen reactions, since most lectins contain at least two saccharide-binding sites per molecule. Because of the carbohydrate-binding specificities of lectins, some of these agglutinins have proven to be quite useful for clinical blood-typing and structural studies of blood-group substances, analysis of cell-surface structure of normal and tumor cells, specific isolation of glycoproteins and oligo- and mucopolysaccharides, studies on mitogenesis, and the localization of specific carbohydrate sequences at the microscopic and ultrastructural level.

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Department of Developmental and Cell Biology, University of California, Irvine, California, USA
Garth L. Nicolson

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Department of Pathology, University of California Medical School, San Diego, La Jolla, California, USA
Stewart Sell

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Nicolson, G.L. (1980). Lectin Interactions with Normal and Tumor Cells and the Affinity Purification of Tumor Cell Glycoproteins. In: Sell, S. (eds) Cancer Markers. Contemporary Biomedicine, vol 1. Humana Press. https://doi.org/10.1007/978-1-4612-6117-9_15

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