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Abstract:
A glcuose-sensitive high-affinity receptor for phlorizin is prseent in isolated brush border membrane of rat kidney and is thought to be the first station in a chain of processes comprising “transmembrane transport of glucose”.
This receptor was labeled with N-[14C]ethylmaleimide for identification and future isolation according to the substrate protection effect. Three molecules of N-[14C]ethylmaleimide are inhibited from the reaction with the bursh border membrane if one high-affinity binding site is protected by phlorizin. d-Glucose also protects the high-affinity phlorizin receptor from the reaction with N-[14C]ethylmaleimide, suggesting that the site labeled is not only part of a phlorizin receptor but also of a glucose binding protein in the brush border membrane.
