Abstract
Binding of 3H-labeled methylated monellin [from Dioscorephyllum cumminsii] to taste receptor tissue was demonstrated in vitro. Preparations of bovine and human circumvallate (taste) papillae bound more of the ligand than did lingual and nonlingual epithelial preparations devoid of taste buds. Binding to the taste preparations saturated at high ligand concentrations. Sugars and other sweet-tasting molecules appeared to compete to some extent with this sweet-tasting protein for its binding sites. These binding measurements of the intensely sweet-tasting protein monellin to taste receptor preparations help to establish the binding interaction as an initial step in taste sensation.