1. The effects of the odorant compounds adenosine-5'-monophosphate (5'AMP), ammonium, betaine, L-cysteine, L-glutamate, DL-succinate, and taurine and of mixtures of these compounds on binding of taurine and 5'AMP to dendritic membrane from the olfactory organ of spiny lobsters (Panulirus argus) were quantified to evaluate the contribution of inhibition of odorant-receptor binding to the generation of physiological responses to mixtures. 2. Taurine binding sites belong to two affinity classes, while 5'AMP binding sites belong to a single affinity class. Binding of either taurine or 5'AMP was partially inhibited in an apparently noncompetitive, concentration dependent fashion by most odorant compounds, with 25-40% inhibition by 1 mM of odorant. Mixtures of two or more odorant compounds also inhibited binding of taurine or 5'AMP to its sites. However, the inhibition by mixtures was often significantly less than expected from the inhibition produced by a mixture's components assuming either a noncompetitive or competitive mechanism. 3. By including this binding inhibition between compounds into models for predicting physiological responses to mixtures from the responses to the components, the predictive power of the models is significantly improved. This result strongly suggests that binding inhibition can influence the physiological responsiveness of chemoreceptor cells to mixtures.

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A unique probe--biotinylated adenosine-5'-monophosphate (5'AMP-biotin)--was used in transmission electron microscopic (TEM) studies to localize 5'AMP odorant binding sites on the dendrites of olfactory receptor neurons in the aesthetasc sensilla of the spiny lobster, Panulirus argus. This probe is capable of both binding to and exciting 5'AMP-sensitive olfactory receptor neurons, as revealed through biochemical and electrophysiological assays. TEM studies showed that 5'AMP-biotin binding sites are distributed along the entire dendritic region that is exposed to odorants, including the transitional zone (between the inner and outer dendritic segments, including the ciliary segment) and all of the outer dendritic segment. The density of 5'AMP binding sites per micron2 of membrane is similar along the length of the olfactory dendrite. However, the relative number of 5'AMP-biotin binding sites per micron2 of sensillar area diminishes in the distal 30% of the aesthetasc due to a decrease in the amount of dendritic membrane in that region. The distribution of these 5'AMP binding sites is therefore much more extensive than that of enzymes that inactivate 5'AMP--5'ectonucleotidase/phosphatase--which are restricted to the transitional zone (Gleeson et al., 1991). Taken together, these results suggest that 5'AMP-biotin is labeling 5'AMP-specific olfactory receptor sites that are located along the entire outer dendritic segment and that can be coupled to olfactory transduction. This study represents the first in situ localization of specific olfactory receptor sites using a specific, functionally defined ligand.

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