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J. Biol. Chem., Vol. 263, Issue 8, 3952-3959, 03, 1988

Sex pheromone receptor proteins. Visualization using a radiolabeled photoaffinity analog

RG Vogt, GD Prestwich and LM Riddiford
Department of Chemistry, State University of New York, Stony Brook 11794-3400.

A tritium-labeled photoaffinity analog of a moth pheromone was used to covalently modify pheromone-selective binding proteins in the antennal sensillum lymph and sensory dendritic membranes of the male silk moth, Antheraea polyphemus. This analog, (E,Z)-6,11-[3H]hexadecadienyl diazoacetate, allowed visualization of a 15-kilodalton soluble protein and a 69-kilodalton membrane protein in fluorescence autoradiograms of electrophoretically separated antennal proteins. Covalent modification of these proteins was specifically reduced when incubation and UV irradiation were conducted in the presence of excess unlabeled pheromone, (E,Z)-6,11-hexadecadienyl acetate. These experiments constitute the first direct evidence for a membrane protein of a chemosensory neuron interacting in a specific fashion with a biologically relevant odorant.
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				M. E. Rogers, M. Sun, M. R. Lerner, and R. G. Vogt Snmp-1, a Novel Membrane Protein of Olfactory Neurons of the Silk Moth Antheraea polyphemus with Homology to the CD36 Family of Membrane Proteins J. Biol. Chem., June 6, 1997; 272(23): 14792 - 14799. [Abstract] [Full Text] [PDF]