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Publication : Cloning and sequence analysis of a hamster liver cDNA encoding a novel putative carboxylesterase.

First Author  Sone T Year  1994
Journal  Biochim Biophys Acta Volume  1207
Issue  1 Pages  138-42
PubMed ID  8043605 Mgi Jnum  J:19544
Mgi Id  MGI:67715 Doi  10.1016/0167-4838(94)90063-9
Citation  Sone T, et al. (1994) Cloning and sequence analysis of a hamster liver cDNA encoding a novel putative carboxylesterase. Biochim Biophys Acta 1207(1):138-42
abstractText  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.
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