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Natural ligands of porcine olfactory binding proteins Inra
Le Danvic, C.; Guiraudie-Capraz, G.; Abderrahmani, D.; Zanetta, J.P.; Nagnan-Le Meillour, P..
Knowledge of endogenous ligands of olfactory binding proteins is a prerequisite for studying their role in odor and pheromone transduction. Here, we report the extraction, derivatization, and characterization by gas chromatography-mass spectrometry of the natural ligands of pig, Sus scrofa (L.), Von Ebner’s Gland protein (VEG) and odorant binding protein (OBP). We identified two isoforms (VEG1 and VEG2), which differed only by the linkage of an O-N-acetylglucosamine (O-GlcNac) group on VEG1. The natural ligands of VEG1 were characterized as two isomers of testosterone, whereas ligands of VEG2 and OBP were fatty acids or their derivatives. Our findings suggest that the binding specificity of VEG1 for steroids is governed by the presence of an O-GlcNac...
Tipo: Journal Article Palavras-chave: MOLÉCULE ODORANTE ENDOGENOUS LIGAND; FATTY ACID; MALDI-TOF MASS SPECTROMETRY; ODORANT BINDING PROTEIN; OLFACTION; O-N-ACETYLGLUCOSAMINE; TESTOSTERONE; TRYTIC DIGESTION; VON EBNER'S GLAND PROTEIN.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20099a3bdd2f&uri=/notices/prodinra1/2010/11/
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Phosphorylation of native porcine olfactory binding proteins Inra
Nagnan-Le Meillour, P.; Le Danvic, C.; Brimau, F.; Chemineau, P.; Michalski, J.C..
The identification of various isoforms of olfactory binding proteins is of major importance to elucidate their involvement in detection of pheromones and other odors. Here, we report the characterization of the phosphorylation of OBP (odorant binding protein) and Von Ebner’s gland protein (VEG) from the pig, Sus scrofa. After labeling with specific antibodies raised against the three types of phosphorylation (Ser, Thr, Tyr), the phosphate-modified residues were mapped by using the beta-elimination followed by Michael addition of dithiothreitol (BEMAD) method. Eleven phosphorylation sites were localized in the pOBP sequence and nine sites in the VEG sequence. OBPs are secreted by Bowman’s gland cells in the extracellular mucus lining the nasal cavity. After...
Tipo: Journal Article Palavras-chave: WESTERN BLOT; SPECTROMETRIE DE MASSE MALDI TOF; BEMAD; GEL DE POLYACRYLAMIDE.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20093ae177c1&uri=/notices/prodinra1/2010/11/
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The insect attractant 1-Octen-3-o1 is the natural ligand of bovine odorant-binding protein Inra
Ramoni, R.; Vincent, F.; Grolli, S.; Conti, V.; Malosse, C.; Boyer, F.D.; Nagnan-Le Meillour, P.; Spinelli, S.; Cambillau, C.; Tegoni, M..
Bovine odorant-binding protein (bOBP) is a dimeric lipocalin present in large amounts in the respiratory and olfactory nasal mucosa. The structure of bOBP refined at 2.0-Å resolution revealed an elongated volume of electron density inside each buried cavity, indicating the presence of one (or several) naturally occurring copurified ligand(s) (Tegoni et al. (1996)Nat. Struct. Biol. 3, 863–867; Bianchet et al.(1996) Nat. Struct. Biol. 3, 934–939). In the present work, by combining mass spectrometry, x-ray crystallography (1.8-Å resolution), and fluorescence, it has been unambiguously established that natural bOBP contains the racemic form of 1-octen-3-ol. This volatile substance is a typical component of bovine breath and in general of odorous body...
Tipo: Journal Article Palavras-chave: TECHNIQUE ANALYTIQUE; SPECTROMÉTRIE DE MASSE; CHROMATOGRAPHIE EN PHASE GAZEUSE; STRUCTURE TRIDIMENSIONNELLE; LIGAND FLUORESCENCE SPECTROSCOPY; URINARY PROTEINS; NASAL-MUCOSA; AFFINITIES; MECHANISM; LIPOCALIN; MOSQUITOS; RECEPTOR.
Ano: 2001 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0200012319094103&uri=/notices/prodinra1/2010/10/
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