Title: | "Biochemical characterization, molecular cloning and localization of a putative odorant-binding protein in the honey bee Apis mellifera L. (Hymenoptera : Apidea)" |
Author(s): | Danty E; Michard-Vanhee C; Huet JC; Genecque E; Pernollet JC; Masson C; |
Address: | "Neurobiologie Experimentale et Theorie des Systemes complexes, CNRS UPR 9081, Paris, France" |
DOI: | 10.1016/s0014-5793(97)01048-x |
ISSN/ISBN: | 0014-5793 (Print) 0014-5793 (Linking) |
Abstract: | "A honey bee antennal water-soluble protein, APS2, was purified and characterized as the first Hymenoptera putative odorant-binding protein. Comparison of its measured Mr (13695.2+/-1.6) to that of the corresponding cDNA clone shows it does not undergo any post-translational modification other than a 19-residue signal peptide cleavage and formation of three disulfide bridges. These biochemical features are close to those of Lepidoptera odorant-binding proteins. In situ hybridization experiments demonstrated its specific expression in olfactory areas. Based on its higher expression in the worker than in the drone, ASP2 might be more involved in general odorant than in sex pheromone detection" |
Keywords: | "Amino Acid Sequence Animals Base Sequence Bees/*chemistry/physiology Behavior, Animal Carrier Proteins/chemistry/*genetics/*metabolism Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel/methods Female In Situ Hybridization Insect Pro;" |
Notes: | "MedlineDanty, E Michard-Vanhee, C Huet, J C Genecque, E Pernollet, J C Masson, C eng Comparative Study Research Support, Non-U.S. Gov't England 1997/10/10 FEBS Lett. 1997 Sep 15; 414(3):595-8. doi: 10.1016/s0014-5793(97)01048-x" |