Neeb M, Fasold H, Koepsell H
FEBS Lett. 1985 Mar 11;182(1):139-44. doi: 10.1016/0014-5793(85)81171-6.
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.
合成了共价结合的D-葡萄糖类似物10-N-(溴乙酰基)氨基-1-癸基-β-D-吡喃葡萄糖苷(BADG),并证明它是肾Na+-D-葡萄糖共转运蛋白的高亲和力抑制剂。从肾刷状缘膜中分离出一种蛋白质组分,其中每毫克蛋白质中Na+-依赖性根皮苷结合位点的浓度富集了7倍。在用该蛋白质组分进行的标记实验中,鉴定出一种分子量约为79000的多肽含有肾Na+-D-葡萄糖共转运蛋白的D-葡萄糖结合位点。