Biochemical studies of olfaction: binding specificity of radioactively labeled stimuli to an isolated olfactory preparation from rainbow trout (Salmo gairdneri).

It is postulated that a multiplicity of types of olfactory binding sites exist in the trout: site TSA, which binds L-threonine, L-serine, and L-alanine; site L, whichbinds L-lysine; and site AB which binds beta-alanines.

Abstract

The extent of binding of 10 radioactively labeled odorant amino acids to a sedimentable fraction (fraction P2) derived from the olfactory rosettes of the rainbow trout Salmo gairdneri corresponded closely with their reported relative stimulatory effectiveness measured electrophysiologically. L isomers were bound to a greater extent than their respective D isomers. Binding of L-alanine was strongly and irreversibly inhibited by mercurials but was not affected by sulfhydryl-blocking reagents. Binding was saturable and reversible. Scatchard analyses gave evidence of two types of binding sites for most of the amino acids studied. The Kd values of the higher-affinity binding sites were similar among the amino acids, being in the range of 10(-6) M; differences occurred in the relative numbers of sites, n. These results, coupled with those from competition experiments, lead to the postulate that a multiplicity of types of olfactory binding sites exist in the trout: site TSA, which binds L-threonine, L-serine, and L-alanine; site L, which binds L-lysine; and site AB which binds beta-alanine. Tentative assignments are: site V, which binds L-valine; site H, which binds L-histidine; and site AD, which binds D-alanine. Site AD may be a lower affinity site for L-alanine. Binding of olfactory stimulus molecules appears to be an initial discrimination step in olfaction.