Molecular cloning and expression of a cDNA encoding an olfactory-specific mouse phenol sulphotransferase
Copyright policy )Molecular cloning and expression of a cDNA encoding an olfactory-specific mouse phenol sulphotransferase
Previously we demonstrated the presence of phenol sulphotransferase (P-ST) in mouse nasal cytosols and identified its zonal location in mouse nasal cavity by staining with an antiserum raised against a rat liver P-ST isoenzyme, PSTg. In the present study a cDNA was isolated from a mouse olfactory cDNA library by immunological screening with the antiserum. The isolated cDNA consisted of 1347 bp with a 912 bp open reading frame encoding a 304-residue polypeptide. Both the nucleotide and deduced amino acid sequences of the cDNA were 94% identical with those of a rat liver P-ST isoenzyme, ST1C1. The expressed enzyme in Escherichia coli displayed high P-ST activity towards phenolic odorants such as eugenol and guaiacol, and it showed a high N-hydroxy-2-acetylaminofluorene sulphation activity in comparison with the rat ST1C1 enzyme. These results indicate that the olfactory P-ST encoded by the cDNA is a mouse orthologue of rat ST1C1; however, expression of the olfactory P-ST mRNA is specific for nasal tissues as revealed by reverse transcriptase-mediated PCR (RT–PCR).
- University of Tokyo Japan
Base Sequence, Sequence Homology, Amino Acid, Guaiacol, Molecular Sequence Data, Hydroxyacetylaminofluorene, Sequence Analysis, DNA, Arylsulfotransferase, Recombinant Proteins, Substrate Specificity, Kinetics, Mice, Nasal Mucosa, Eugenol, Escherichia coli, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Sequence Alignment, Phylogeny
Base Sequence, Sequence Homology, Amino Acid, Guaiacol, Molecular Sequence Data, Hydroxyacetylaminofluorene, Sequence Analysis, DNA, Arylsulfotransferase, Recombinant Proteins, Substrate Specificity, Kinetics, Mice, Nasal Mucosa, Eugenol, Escherichia coli, Animals, Amino Acid Sequence, RNA, Messenger, Cloning, Molecular, Sequence Alignment, Phylogeny
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