Binding of soybean agglutinin to glycolipid components of porcine lymphocyte plasma membranes |
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Authors: | Harvey J. Sage Lynn D. Yates Curley B. Horton |
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Affiliation: | VA Hospital and Biochemistry Department, Duke University Medical Center, Durham, North Carolina 27705 U.S.A. |
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Abstract: | 125I-Labeled soybean agglutinin binds primarily to glycolipids contained in pig lymphocyte plasma membranes as measured by in situ “staining” of membranes subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Separation of these glycolipids by differential extraction, silicic acid chromatography, and high-performance thin-layer chromatography showed that three different species of plasma membrane glycolipid bind this lectin; trihexosyl ceramide, globoside, and ganglioside GM2 in order of increasing affinity (over a range of 10- to 20-fold). Trihexosyl ceramide and globoside, major neutral membrane glycolipids, are the major binders; while GM2, a minor acidic glycolipid, is a quantitatively smaller lectin-binding component. |
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Keywords: | Author to whom all correspondence should be sent. |
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