Danty E, Michard-Vanhée C, Huet J C, Genecque E, Pernollet J C, Masson C
Neurobiologie Expérimentale et Théorie des Systèmes complexes, CNRS UPR 9081, Paris, France.
FEBS Lett. 1997 Sep 15;414(3):595-8. doi: 10.1016/s0014-5793(97)01048-x.
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.
一种蜜蜂触角水溶性蛋白APS2被纯化，并被鉴定为膜翅目首个假定的气味结合蛋白。将其测得的相对分子质量（13695.2±1.6）与相应cDNA克隆的相对分子质量进行比较，结果表明，除了一个19个残基的信号肽被切割以及形成三个二硫键外，它没有经历任何翻译后修饰。这些生化特征与鳞翅目气味结合蛋白的特征相近。原位杂交实验证明了它在嗅觉区域的特异性表达。基于其在工蜂中比在雄蜂中表达更高，ASP2可能更多地参与一般气味的检测而非性信息素的检测。
