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Abstract
The brushborder membrane of the proximal convolution contains a phlorizin binding site, which due to its high affinity for phlorizin and other properties like competitive inhibition by D-glucose and sodium dependence has been suggested to be involved in the transport of D-glucose through the brushborder membrane [l-3] In order to study the chemical and physical interactions between this receptor and the transported substrate an extraction and purification of the molecule is important. In this paper a procedure is described by which the glucose sensitive phlorizin binding site can be extracted from the membranes in a conformation which still shows the glucose sensitive phlorizin binding The binding itself is measured by a technique in which after the separation of the proteins by electrophoresis the gel is incubated with [3H]phIorizin and [ “C]mannose and after washing.the ratio 3H/14C is determined in the gel slices.
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