Identification of the D-glucose binding polypeptide of the renal Na+-D-glucose cotransporter with a covalently binding D-glucose analog.
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.
D000117:Acetylglucosamine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D000345:Affinity Labels / Q000138:chemical synthesis / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D005944:Glucosamine / Q000031:analogs & derivatives*; D007668:Kidney / Q000378:metabolism* / Q000648:ultrastructure; D008871:Microvilli / Q000378:metabolism; D008970:Molecular Weight; D009004:Monosaccharide Transport Proteins; D010695:Phlorhizin / Q000494:pharmacology; D012964:Sodium / Q000378:metabolism*; D013552:Swine
D000345:Affinity Labels; D002352:Carrier Proteins; D009004:Monosaccharide Transport Proteins; C044848:10-N-(bromoacetyl)amino-1-decylglucopyranoside; D012964:Sodium; D010695:Phlorhizin; D005944:Glucosamine; D000117:Acetylglucosamine