Cloning and expression of human liver rhodanese cDNA.
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Aita N, Ishii K, Akamatsu Y, Ogasawara Y, Tanabe S
Cloning and expression of human liver rhodanese cDNA.
Biochem Biophys Res Commun. 1997 Feb 3;231(1):56-60.
- PubMed ID
- 9070219 [ View in PubMed]
- Abstract
cDNA for the human rhodanese (thiosulfate; cyanide sulfurtransferase, EC 2.8.1.1) was cloned from a human fetal liver cDNA library. Sequencing of the cDNA revealed an open reading frame that encodes a 297-residue polypeptide with a calculated mass of 33,427 daltons. When the rhodanese cDNA was transiently expressed in Escherichia coli and Cos7 cells, the rhodanese activity increased 40-fold and 150-fold, respectively. Sequence homology analysis showed that the human rhodanese is 89.6% identical to bovine, 90.2% identical to rat, 91.2% identical to mouse and Chinese hamster, and 71.4% similar to avian counterparts, respectively, and that rhodanese was highly conserved across evolution.