The surface glycoproteins of human skin fibroblasts detected after electrophoresis by the binding of peanut (Arachis hypogaea) agglutinin and Ricinus communis (castor-bean) agglutinin I.

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Abstract
A new methodology was developed to study the cell-surface glycoproteins of cultured human skin fibroblasts. This was based on the binding of a variety of biotinyl lectins to nitrocellulose electrophoretic transfers of total fibroblast lysates after separation in sodium dodecyl sulfate/polyacrylamide gels, followed by reaction with avidin-biotinyl peroxidase complexes and detection with 3,3''-diaminobenzidine. The technique proved to be very sensitive and a large number of glycoproteins were detected by binding of concanavalin A and wheat germ agglutinin. Binding of peanut agglutinin and to a lesser extent of R. communis agglutinin I were dependent on prior removal of sialic acid residues from the glycoproteins. Since by treatment of intact viable cells with neuraminidase only external sialic acid residues were removed, peanut agglutinin and R. communis agglutinin I could thus be utilized for selective detection of cell-surface glycoproteins. Because peanut agglutinin was known to bind preferentially to oligosaccharides to the O-glycosidic type, and R. communis agglutinin I to those of the N-glycosidic type, the 2 lectins were complementary in displaying the surface glycoproteins and in providing information about their oligosaccharide composition.