Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous Abstract"Degradation of an alkaloid pheromone from the pale-brown chafer, Phyllopertha diversa (Coleoptera: Scarabaeidae), by an insect olfactory cytochrome P450"    Next Abstract"Is 3D printing safe? Analysis of the thermal treatment of thermoplastics: ABS, PLA, PET, and nylon" »

Biochem Biophys Res Commun


Title:Identification and cloning of odorant binding proteins from the scarab beetle Phyllopertha diversa
Author(s):Wojtasek H; Picimbon JF; Soares Leal W;
Address:"Laboratory of Chemical Prospecting, National Institute of Sericultural and Entomological Science, 1-2 Ohwashi, Tsukuba, 305-8634, Japan"
Journal Title:Biochem Biophys Res Commun
Year:1999
Volume:263
Issue:3
Page Number:832 - 837
DOI: 10.1006/bbrc.1999.1448
ISSN/ISBN:0006-291X (Print) 0006-291X (Linking)
Abstract:"Wehave identified, cloned, and characterized two odorant binding proteins from the pale brown chafer, Phyllopertha diversa. One of the proteins (OBP1, 116 amino acids long) showed high amino acid identity (>90%) to two previously identified PBPs from scarab beetles. The second protein (OBP2) showed limited sequence similarity to lepidopteran and dipteran OBPs, but contained only 133 amino acids. Both proteins showed the occurrence of six highly conserved cysteines; electrospray mass spectral data suggested they are all bound in three disulfide bonds. During purification, OBP2 separated into several isoforms; N-terminal amino acid sequencing and electrospray ionization mass spectrometry demonstrated that they are different conformations of the same protein. In the native gel electrophoresis binding experiments, none of the OBPs bound 1, 3-dimethyl-2,4-(1H,3H)-quinazolinedione but different isoforms showed different binding affinities for (R)-japonilure, a pheromone from related scarab beetles, and bombykol, the pheromone from the silkworm moth, Bombyx mori. OBP1 also bound (R)-japonilure"
Keywords:"Amino Acid Sequence Animals Cloning, Molecular Coleoptera/genetics/*physiology Molecular Sequence Data Molecular Weight *Odorants Receptors, Odorant/*chemistry/*genetics/isolation & purification Recombinant Proteins/biosynthesis/isolation & purification S;"
Notes:"MedlineWojtasek, H Picimbon, J F Soares Leal, W eng Research Support, Non-U.S. Gov't 1999/10/08 Biochem Biophys Res Commun. 1999 Oct 5; 263(3):832-7. doi: 10.1006/bbrc.1999.1448"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 06-07-2024