Sex pheromone receptor proteins. Visualization using a radiolabeled photoaffinity analog.

التفاصيل البيبلوغرافية
العنوان: Sex pheromone receptor proteins. Visualization using a radiolabeled photoaffinity analog.
المؤلفون: Vogt, R G, Prestwich, G D, Riddiford, L M
المصدر: Journal of Biological Chemistry; March 1988, Vol. 263 Issue: 8 p3952-3959, 8p
مستخلص: 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.
قاعدة البيانات: Supplemental Index
الوصف
تدمد:00219258
1083351X
DOI:10.1016/S0021-9258(18)69018-0