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Cloning and sequence analysis of a cDNA encoding tetrameric carbonyl reductase of pig lung.

Abstract：

:A cDNA for tetrameric carbonyl reductase was cloned from a pig lung cDNA library. The cDNA had an open reading frame encoding a protein of 244 amino acid residues with a predicted monomer molecular weight of 25,985. The authenticity of the cDNA was confirmed by a perfect match of 80 amino acids determined from sequencing of amino-terminus, carboxy-terminus and internal fragments of the purified enzyme. The deduced sequence of the carbonyl reductase shows a similarity to those of the short-chain alcohol dehydrogenase superfamily proteins; notably it had an extensive homology (85% identical residues) with a putative gene product of murine adipocyte.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Nakanishi M,Deyashiki Y,Nakayama T,Sato K,Hara A

doi

10.1006/bbrc.1993.1967

subject

Has Abstract

pub_date

1993-08-16 00:00:00

pages

1311-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71967-4

journal_volume

194

pub_type

杂志文章

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