Taste receptor proteins

Abstract

The chemistry of taste has eluded widespread investigation until only recently. Of the four basic taste qualities — sweet, salty, sour and bitter, only sweet and to some lesser extent — bitter — have had inroads made on the molecular level. Carbon-14 labeled sugars are preferently bound to taste bud proteins versus other non-sensory proteins. The binding of the sugars is in good agreement with their relative sweetness and graded conformational changes in protein molecules are seen, by a number of methods, upon these interactions. The protein may occur in two forms — soluble and membrane bound, and the bound form can be solubilized. Unique proteins are present in taste buds and would thus differentiate them from other non-sensory proteins. The sweet-sensitive protein activity has been studied in a number of animals, but purification and characterization in all has not proceeded to the point wherein comparisons can be made. Bitter reception has been suggested as the property of a protein from pig tongues, and an enzyme — phosphodiesterase has been found to be both activated and inhibited by bitter compounds. Lipids from gustatory tissue have been suggested as candidates for receptors for salty, sour and bitter, but not sweet stimulants.