Tuccini A, Maida R, Rovero P, Mazza M, Pelosi P
Istituto di Industrie Agrarie, Pisa, Italy.
Insect Biochem Mol Biol. 1996 Jan;26(1):19-24. doi: 10.1016/0965-1748(95)00051-8.
A 19 kDa protein has been purified by gel filtration and anion-exchange chromatography from the antennae of Carausius morosus. Its amino terminal amino acid sequence shows significant similarity (30% identity) with another putative odorant-binding protein, the so called OS-D protein isolated from the antennae of Drosophila melanogaster; only 20% of its amino acids are shared with some members of Lepidoptera pheromone-binding proteins. Polyclonal antibodies, raised against a synthetic amino terminal peptide cross-react with 19 kDa band in the legs extracts, but not with soluble proteins from other parts of the body. The amino terminal sequence of this protein, purified from the legs was identical with that of the antennal protein.
