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Cloning and sequence analysis of a hamster liver cDNA encoding a novel putative carboxylesterase
T Sone1, M Isobe, E Takabatake
1Department of Toxicology, Faculty of Pharmaceutical Sciences, Setsunan University, Osaka, Japan.
Biochimica Et Biophysica Acta
|July 20, 1994
Abstract:
A full-length cDNA encoding for a putative carboxylesterase was isolated from a hamster liver cDNA library. The cDNA consisting of 1911 base pairs contained an open reading frame of 1683 base pairs encoding for a polypeptide of 561 amino-acid residues, including 27 N-terminal amino-acid residues for signal peptide. The deduced amino-acid sequence of the cDNA is in 67% homology with the amino-acid sequence of rabbit form 2 carboxylesterase, which has not yet been cloned. It also had many structural features highly conserved among carboxylesterase isozymes.