Demonstration of glucose inhibitable phlorizin binding to renal brushborder 
proteins separated by gel electrophoresis

Thomas, Lothar

doi:10.1016/0014-5793(72)80495-2

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Demonstration of glucose inhibitable phlorizin binding to renal brushborder proteins separated by gel electrophoresis

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Thomas, Lothar
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Thomas, L. (1972). Demonstration of glucose inhibitable phlorizin binding to renal brushborder proteins separated by gel electrophoresis. FEBS Letters, 25(2), 245-248. doi:10.1016/0014-5793(72)80495-2.

Cite as: https://hdl.handle.net/21.11116/0000-0008-B827-D

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. 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 [¹⁴C]mannose and after washing the ratio [³H/[¹⁴C is determined in the gel slices.