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Immunocytochemistry of Odorant-Binding Proteins
1994Odorant-binding proteins are small water-soluble proteins that have been detected in the perireceptor compartment of olfactory receptor cells of vertebrates and insects [1,2]. Although their definite physiological role in olfaction is still unclear, similar functions have been proposed in stimulus transport or inactivation [1–6].
Steinbrecht, R. +3 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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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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Stability and Dynamics of the Porcine Odorant-Binding Protein
Biochemistry, 2007The 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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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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Odorant‐Binding Proteins: Expression and Function
Annals of the New York Academy of Sciences, 1998ABSTRACT: 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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International Journal of Biological Macromolecules, 2021
The GOBP2 protein has a unique function in the yellow peach moth (Conogethes punctiferalis (Guenée)). Several general odorant-binding proteins (GOBPs) have been identified in various lepidopteran species, but the functional difference between GOBP1 and ...
Dapeng Jing +5 more
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The GOBP2 protein has a unique function in the yellow peach moth (Conogethes punctiferalis (Guenée)). Several general odorant-binding proteins (GOBPs) have been identified in various lepidopteran species, but the functional difference between GOBP1 and ...
Dapeng Jing +5 more
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Isoleucine residues determine chiral discrimination of odorant-binding protein.
Chemistry, 2020Enzymes, receptors and carrier proteins discriminate between enantiomers of natural and synthetic chemicals. While the structural details of this phenomenon have been investigated in enzymes and receptors, much less is known for carrier proteins of ...
Valeriia Zaremska +4 more
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Journal of Agricultural and Food Chemistry, 2019
Odorant binding proteins (OBPs) are considered to be highly expressed at antennae sensillum lymph and play crucial roles in detection of insect host plant volatiles.
Hangwei Liu +7 more
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Odorant binding proteins (OBPs) are considered to be highly expressed at antennae sensillum lymph and play crucial roles in detection of insect host plant volatiles.
Hangwei Liu +7 more
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Conformational Isomers of Insect Odorant-Binding Proteins
Archives of Biochemistry and Biophysics, 2002We 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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