Antisera prepared in rabbit to a D-glucose-inhibitable phlorizin binding component of the pig kidney brush border membrane precipitated more than 90 percent of the D-glucose-inhibitable phlorizin binding activity from a Triton extract. These antibodies also stimulated D-glucose uptake by native brush border membranes at low D-glucose concentrations (1 mM) and inhibited it at higher D-glucose concentrations. Immunoblotting was used to locate polypeptide subunits of the glucose transporter in polyacrylamide gels of proteins extracted from the brush border membranes. The antibodies labelled the Mr 70,000 phlorizin-binding component in both reducing and non reducing conditions. Two additional polypeptides with relative molecular mass of 120,000 and 45,000 were also recognized under the same conditions; they might correspond, respectively, to another Na+/D-glucose cotransport unit and to a post mortem degradation product.