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Journal Article

Identification of the D-glucose binding polypeptide of the renal Na+-D-glucose cotransporter with a covalently binding D-glucose analog

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Neeb,  Martin
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Koepsell,  Hermann
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Neeb, M., Fasold, H., & Koepsell, H. (1985). Identification of the D-glucose binding polypeptide of the renal Na+-D-glucose cotransporter with a covalently binding D-glucose analog. FEBS Letters, 182(1), 139-144. doi:10.1016/0014-5793(85)81171-6.


Cite as: https://hdl.handle.net/21.11116/0000-0008-053C-0
Abstract
The covalently binding D-glucose analog 10-N-(bromoacetyl)amino-1-decyl-beta-D-glucopyranoside (BADG) was synthesised and shown to be a high-affinity inhibitor of the renal Na+-D-glucose contransporter. From renal brush-border membranes a protein fraction was isolated, in which the concentration of Na+-dependent phlorizin binding sites per mg protein was enriched 7-fold. In labeling experiments with this protein fraction a polypeptide of Mr approximately 79000 was identified as containing the D-glucose binding site of the renal Na+-D-glucose cotransporter.