Biochemical characterization, molecular cloning and localization of a putative odorant‐binding protein in the honey bee Apis mellifera L. (Hymenoptera: Apidea)

FEBS Letters

Pernollet, J.-C.¹  Huet, J.-C.¹  Michard-Vanhée, C.²  Masson, C.²  Genecque, E.²  Danty, E.² 

[1] Unité de Recherches de Biochimie et Structure des Protéines, INRA UR 477, Domaine de Vilvert, F78352 Jouy-en-Josas Cedex, France;Neurobiologie Expérimentale et Théorie des Systèmes complexes, CNRS UPR 9081, 16, rue Claude Bernard, F-75231 Paris Cedex 05, France

关键词: Odorant-binding protein;    Post-translational modification;    Sequence;    Sexual dimorphism;    Antenna;    Apis mellifera L.;    DIG;    digoxigenin;    GOBP;    general odorant-binding protein;    IS-MS;    ion-spray mass spectrometry;    OBP;    odorant-binding protein;    PBP;    pheromone-binding protein;    RPLC;    reverse-phase high performance liquid chromatography;   

DOI  :  10.1016/S0014-5793(97)01048-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A honey bee antennal water-soluble protein, APS2, was purified and characterized as the first Hymenoptera putative odorant-binding protein. Comparison of its measured M _r (13 695.2±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.

【 授权许可】

Unknown