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. 1994 Jul 20;1207(1):138-42.
doi: 10.1016/0167-4838(94)90063-9.

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

T Sone  1 , M Isobe, E Takabatake, C Y Wang
Affiliations

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

T Sone et al. Biochim Biophys Acta. .

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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