Periodate induced cross-linking of concanavalin A-reactive membrane proteins of rabbit thymocytes.
Purified plasma membranes of rabbit thymocytes are exposed to sodium periodate and galactose oxidase at conditions similar to those used to induce mitogenic transformation of lymphocytes. The membrane proteins are then fractionated by dodecyl sulfate poly-acrylamide gel electrophoresis. At concentrations of 0.005 M, Na IO4 cross-links 55,000 D and 110,000 D glycoproteins which are known to specifically bind concanavalin A. Galactose oxidase has a similar cross-linking effect, but, at the same time causes proteolytic degradation of membrane proteins. Our data indicate that oxidizing agents, like NaIO4 and galactose oxidase, can indeed cross-link receptors of the thymocyte plasma membrane as has often been proposed as a possible mechanism of their action.
D000818:Animals; D002462:Cell Membrane / Q000187:drug effects*; D005260:Female; D005692:Galactose Oxidase / Q000494:pharmacology; D006023:Glycoproteins / Q000378:metabolism; D010504:Periodic Acid / Q000494:pharmacology*; D011817:Rabbits; D011952:Receptors, Concanavalin A / Q000187:drug effects* / Q000378:metabolism; D011955:Receptors, Drug / Q000187:drug effects*; D013347:Subcellular Fractions; D013601:T-Lymphocytes
D006023:Glycoproteins; D011952:Receptors, Concanavalin A; D011955:Receptors, Drug; D010504:Periodic Acid; D005692:Galactose Oxidase