Abstract
A number of glycosides structurally related to phlorizin have been tested for biological activity. Their influence on the renal tubular reabsorption of glucose in the dog has been compared with the inhibitory capacity exhibited by phlorizin. Some conclusions concerning the nature of the critical structural and geometrical configuration of the inhibitor molecule are presented. Some information has been obtained on the mechanism of phlorizin inhibition at a molecular level and on the nature and topography of the chemical groups constituting the receptor site on the cell membrane to which the inhibitor is bound.
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