Results 181 to 190 of about 18,714 (215)
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Odorant‐Binding Proteins: Expression and Function

Annals of the New York Academy of Sciences, 1998
ABSTRACT: Odorant‐binding proteins (OBPs) are a major constituent of the aqueous perireceptor compartment in vertebrates and in insects. Although different in primary structure, they are supposed to serve similar functions in both animal groups: (i) OBPs may act as solubilizers and carriers of the lipophilic odorants in the aqueous mucus or sensillum ...
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Odorant Binding to Bovine Odorant Binding Protein Detected by Intrinsic Fluorescence

Chemistry Letters, 2005
Abstract 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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Stability and Dynamics of the Porcine Odorant-Binding Protein

Biochemistry, 2007
The denaturation process of porcine odorant-binding protein (pOBP) was studied by intrinsic fluorescence analysis and far- and near-UV circular dichroism measurements. Our results showed that a reversible one-step process described the denaturation by GdnHCl.
Staiano M   +8 more
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Conformational Stability and Binding Properties of Porcine Odorant Binding Protein

Biochemistry, 1999
Apparently homogeneous odorant binding protein purified from pig nasal mucosa (pOBP) exhibited subunit molecular masses of 17 223, 17 447, and 17 689 (major component) Da as estimated by ESI/MS. According to gel filtration, this protein, its truncated forms, and/or its variants are homodimeric under physiologic conditions (pH 6-7, 0.1 M NaCl).
Burova, T.V.   +3 more
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Effects of antibodies against odorant binding proteins on electrophysiological responses to odorants

Biochimica et Biophysica Acta (BBA) - General Subjects, 1988
Monoclonal antibodies against two olfactory mucosal proteins, one with affinity for anisole-like and the other for benzaldehyde-like compounds, were applied to mouse olfactory epithelium. Responses to three odorants (anisole, benzaldehyde and amyl acetate) were measured.
S, Price, A, Willey
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Conformational Isomers of Insect Odorant-Binding Proteins

Archives of Biochemistry and Biophysics, 2002
We have identified and cloned the cDNAs encoding odorant-binding proteins (OBPs) from the large black chafer, Holotrichia parallela, and the yellowish elongate chafer, Heptophylla picea. Each species possess two OBPs, the proteins migrating faster in native gels (OBP1) showed high amino acid identity (>88%) to previously identified pheromone-binding ...
Zhang, Deyu, Walter Soares, Leal
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Site-directed mutagenesis of odorant-binding proteins

2020
Modifying the affinity of odorant-binding proteins (OBPs) to small ligands by replacement of specific residues in the binding pocket may lead to several technological applications. Thanks to their compact and stable structures, OBPs are currently regarded as the best candidates to be used in biosensing elements for odorants and volatiles detection. The
Jiao, Zhu   +4 more
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Odorant-Binding Proteins from a Primitive Termite

Journal of Chemical Ecology, 2002
Hitherto, odorant-binding proteins (OBPs) have been identified from insects belonging to more highly evolved insect orders (Lepidoptera, Coleoptera, Diptera, Hymenoptera, and Hemiptera), whereas only chemosensory proteins have been identified from more primitive species, such as orthopteran and phasmid species.
Yuko, Ishida   +3 more
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Structure and biotechnological applications of odorant-binding proteins

Applied Microbiology and Biotechnology, 2013
Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are folded into α-helical domains.
Pelosi, Paolo   +4 more
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Odorant binding protein 3 is associated with nitenpyram and sulfoxaflor resistance in Nilaparvata lugens

International Journal of Biological Macromolecules, 2022
Kaikai Mao, Zhijie Ren, Ruoheng Jin
exaly  

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