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Critical Reviews in Biochemistry and Molecular Biology, 1994
Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Odorant-binding proteins (OBPs) are low-molecular-weight soluble proteins highly concentrated in the nasal mucus of vertebrates and in the sensillar lymph of insects. Their affinity toward odors and pheromones suggests a role in olfactory perception, but their physiological function has not been clearly defined.
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Odorant‐Binding Proteins: Structural Aspects
Annals of the New York Academy of Sciences, 1998ABSTRACT: Structural data on odorant‐binding proteins (OBPs), both in vertebrates and in insects, are reviewed and discussed. OBPs are soluble proteins interacting with odor molecules and Pheromones in the perireceptor areas, the nasal mucus in vertebrates and the sensillar lymph in insects.
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Binding of selected odorants to bovine and porcine odorant-binding proteins
Chemical Senses, 1993Twenty floral smelling tetrahydropyranyl and tetrahydrofuranyl ethers, and 12 additional compounds with different odours were used in ligand-binding experiments with purified 19 kDa bovine OBP and 22 kDa porcine OBP. Most of the odorants examined were found to be good ligands for both proteins, with dissociation constants in the micromolar range; the ...
DAL MONTE, MASSIMO +3 more
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Odorant-binding proteins of the mouse
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1995After the isolation of two odorant-binding proteins (OBP-I and OBP-II) from mouse nasal tissue, we have purified two additional OBPs, which bind tritiated 2-isobutyl-3-methoxypyrazine. OBP-III is a homodimer with subunits of M(r) 22,000 and pI 4.2. OBP-IV is a homodimer with subunits of M(r) 21,000 and pI 4.85.
PES D, PELOSI, PAOLO
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DyBOBS: A Dynamic Biomimetic Assay for Odorant-Binding to Odor-Binding Protein
Chemosensory Perception, 2010An in vitro system was developed to mimic the structural and flow conditions of the human olfactory epithelium and to measure the dynamics of odorant-binding to odor-binding protein (OBP). A hydrophilic fused silica capillary, coated internally with a thin (about 1.3 µm) aqueous film of recombinant rat-OBP3 mimicked the human olfactory epithelium ...
Yabuki, Masayuki +4 more
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Odorant binding proteins of Heliothis virescens
Insect Biochemistry and Molecular Biology, 1993cDNA clones coding for three different binding proteins were isolated from an antennal library of Heliothis virescens. The deduced amino acid sequences showed only moderate homology to each other but shared several common structural features. Based on a comparison with the predicted primary structures of antennal binding proteins from different moth ...
J, Krieger +3 more
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Electrochemical biosensing with odorant binding proteins
2020The development of sensors that mimic the natural smell sensing mechanism and selectively recognizes the odorants remains highly challenging. Electrochemical based sensing approaches aiming at monitoring molecular recognition events between surface receptors and analytes in solution or in the gas phase, are one possible transduction platforms among ...
Szunerits, Sabine +2 more
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Subtypes of odorant‐binding proteins
European Journal of Biochemistry, 1998Odorant‐binding proteins (OBP) in the mucus of the olfactory epithelium are thought to transfer the hydrophobic odorous compounds through the aqueous barrier towards the chemo‐sensory cells. To evaluate their binding properties, two distinct OBP subtypes of the rat were expressed as N‐terminal His‐tagged fusion proteins in Escherichia coli, thus ...
Lobel D +4 more
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Odorant Binding to Bovine Odorant Binding Protein Detected by Intrinsic Fluorescence
Chemistry Letters, 2005Abstract Odorant binding to bovine odorant binding protein (OBPb) made OBPb structure a little tighter and odorant detection by intrinsic fluorescence possible. For odorant with high affinity such as 3,7-dimethyl-1-octanol (DMO), the binding reaction proceeded in a two-step manner that inferred an existence of a third binding site.
Mineo Ikematsu +2 more
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Pesticide Biochemistry and Physiology, 2022
The Liriomyza trifolii is a highly invasive polyphagia pest. Understanding the physiological functions of odorant binding proteins (OBPs) in the chemical communication of L. trifolii can lead to effective pest management strategies. Seven full-length OBPs were identified by transcriptome screening of L. trifolii adults.
Qikai, Zhang +6 more
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The Liriomyza trifolii is a highly invasive polyphagia pest. Understanding the physiological functions of odorant binding proteins (OBPs) in the chemical communication of L. trifolii can lead to effective pest management strategies. Seven full-length OBPs were identified by transcriptome screening of L. trifolii adults.
Qikai, Zhang +6 more
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