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Immunocytochemistry of Odorant-Binding Proteins

1994
Odorant-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, 1993
cDNA 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, 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
openaire   +1 more source

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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Odorant‐Binding Proteins: Structural Aspects

Annals of the New York Academy of Sciences, 1998
ABSTRACT: 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, 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 ...
openaire   +3 more sources

Genetic knockout and general odorant-binding/chemosensory protein interactions: Revealing the function and importance of GOBP2 in the yellow peach moth's olfactory system.

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
semanticscholar   +1 more source

Isoleucine residues determine chiral discrimination of odorant-binding protein.

Chemistry, 2020
Enzymes, 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
semanticscholar   +1 more source

Key Amino Residues Determining Binding Activities of the Odorant Binding Protein AlucOBP22 to Two Host Plant Terpenoids of Apolygus lucorum.

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
semanticscholar   +1 more source

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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