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  • Title: Cloning and sequence analysis of a hamster liver cDNA encoding a novel putative carboxylesterase.
    Author: Sone T, Isobe M, Takabatake E, Wang CY.
    Journal: Biochim Biophys Acta; 1994 Jul 20; 1207(1):138-42. PubMed ID: 8043605.
    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.
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