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J Chem Ecol


Title:Selective and pH-dependent binding of a moth pheromone to a pheromone-binding protein
Author(s):Leal WS; Chen AM; Erickson ML;
Address:"Maeda-Duffey Laboratory, Department of Entomology, University of California, Davis, CA 95616, USA. wsleal@ucdavis.edu"
Journal Title:J Chem Ecol
Year:2005
Volume:20050928
Issue:10
Page Number:2493 - 2499
DOI: 10.1007/s10886-005-7458-4
ISSN/ISBN:0098-0331 (Print) 0098-0331 (Linking)
Abstract:"Fluorescence and circular dichroism (CD) data suggest that the major pheromone-binding protein (PBP) from the wild silkmoth, Antheraea polyphemus, ApolPBP1, undergoes a pH-dependent conformational change similar to that previously observed for the PBP from the silkworm moth, Bombyx mori, BmorPBP. All three constituents of the sex pheromone, E6,Z11-16Ac, E6,Z11-16Ald, and E4,Z9-14Ac, bound to ApolPBP1 with apparent high affinity at high pH, but reduced binding at low pH when tested individually in a 'cold binding assay.' In competitive assays, however, ApolPBP1 showed considerable preference for the major constituent of the sex pheromone, E6,Z11-16Ac. These data suggest that specificity of PBPs contributes at least in part to the remarkable selectivity of moth's olfactory system"
Keywords:Animals Carrier Proteins/chemistry/*metabolism Circular Dichroism *Hydrogen-Ion Concentration Insect Proteins/chemistry/*metabolism Intercellular Signaling Peptides and Proteins Moths/*chemistry/metabolism Pheromones/chemistry/*metabolism Protein Binding;
Notes:"MedlineLeal, Walter S Chen, Angela M Erickson, Melissa L eng 2005/09/01 J Chem Ecol. 2005 Oct; 31(10):2493-9. doi: 10.1007/s10886-005-7458-4. Epub 2005 Sep 28"

 
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