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 AbstractBiochemical and chemical supports for a transnatal olfactory continuity through sow maternal fluids    Next AbstractFunctional characterization of olfactory binding proteins for appeasing compounds and molecular cloning in the vomeronasal organ of pre-pubertal pigs »

J Biotechnol


Title:Heterologous expression of piglet odorant-binding protein in Pichia pastoris: a comparative structural and functional characterization with native forms
Author(s):Guiraudie-Capraz G; Clot-Faybesse O; Pageat P; Malosse C; Cain AH; Ronin C; Nagnan-Le Meillour P;
Address:"Pherosynthese SA, Le Rieu Neuf, F-84490 Saint-Saturnin-Les-Apt, France. gaelle.guiraudie-capraz@up.univ-mrs.fr"
Journal Title:J Biotechnol
Year:2005
Volume:117
Issue:1
Page Number:11 - 19
DOI: 10.1016/j.jbiotec.2005.01.005
ISSN/ISBN:0168-1656 (Print) 0168-1656 (Linking)
Abstract:"This study targets to express the piglet odorant-binding protein (plOBP) and compare the engineered product to the corresponding native protein forms, i.e. plOBP and adult porcine OBP (pOBP). Using the natural signal peptide from the cDNA sequence, up to 40 mg l(-1) of secreted recombinant piglet OBP (rOBP) has been produced in a minimal culture medium. No significant difference in molecular mass between rOBP and native plOBP could be observed by mass spectrometry following or not trypsin digestion. rOBP and pOBP shared similar immunoreactivity towards polyclonal anti-pOBP antibodies, suggesting a proper processing and folding of the recombinant product. Both plOBP and rOBP displayed comparable binding properties towards fatty acids present in the putative maternal pheromone and a steroid, component of the boar sex pheromone. Furthermore, the rOBP product was found to bind to an olfactory receptor, for which pOBP binding was previously characterized. Taken together, these findings suggest that rOBP, produced in Pichia pastoris, exhibits structural and functional properties comparable to those of the native lipocalins from both young or adult animal"
Keywords:"Animals Pichia/*genetics Receptors, Odorant/chemistry/*genetics/physiology Recombinant Proteins/biosynthesis/chemistry/metabolism Swine;"
Notes:"MedlineGuiraudie-Capraz, Gaelle Clot-Faybesse, Olivier Pageat, Patrick Malosse, Christian Cain, Anne-Helene Ronin, Catherine Nagnan-Le Meillour, Patricia eng Comparative Study Research Support, Non-U.S. Gov't Netherlands 2005/04/16 J Biotechnol. 2005 Apr 20; 117(1):11-9. doi: 10.1016/j.jbiotec.2005.01.005"

 
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 26-12-2024