Primary structure of a pheromone-binding protein from Antheraea pernyi: homologies with other ligand-carrying proteins |
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Authors: | K Raming J Krieger H Breer |
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Institution: | (1) Institut für Zoophysiologie, Universität Stuttgart-Hohenheim, Garbenstr. 30, W-7000 Stuttgart 70, Germany |
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Abstract: | Summary An antennal cDNA clone encoding the complete sequence (163 amino acids) of a pheromone-binding protein precursor from the male silk moth, Antheraea pernyi, was isolated using oligonucleotide probes. The cloned cDNA was expressed and the translation product detected by specific antibodies. The deduced protein sequence consists of a signal peptide of 21 amino acids and a mature binding protein of 142 amino acid residues. The predicted structure of this protein is homologous to binding-proteins from different insect species which have previously been identified, but shows no similarities to odorant-binding proteins from vertebrates, suggesting that soluble odorant-binding proteins in insects and vertebrates represent an evolutionary convergence.Abbreviations
PBP
pheromone-binding protein
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OBP
odorant-binding protein
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cDNA
complentary DNA
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poly(A
+) RNA
polyadenylated RNA
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SSC
0.15 M sodium chloride+0.015 M sodium citrate
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SDS-PAGE
sodium dodecylsulfate polyacrylamide gelelectrophoresis |
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Keywords: | Antheraea Binding-protein Molecular cloning Sequence homologies Expression |
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