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N-Ethylmaleimide labeling of a phlorizin-sensitive D-glucose binding site of brush border membrane form the rat kidney

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Thomas,  Lothar
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Kinne,  Rolf
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Frohnert,  Peter P.
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Thomas, L., Kinne, R., & Frohnert, P. P. (1972). N-Ethylmaleimide labeling of a phlorizin-sensitive D-glucose binding site of brush border membrane form the rat kidney. Biochimica et Biophysica Acta-Biomembranes, 290(1), 125-133. doi:10.1016/0005-2736(72)90057-0.


Cite as: http://hdl.handle.net/21.11116/0000-0008-B8BA-7
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.