| First Author | Aita N | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 231 |
| Issue | 1 | Pages | 56-60 |
| PubMed ID | 9070219 | Mgi Jnum | J:38264 |
| Mgi Id | MGI:85641 | Doi | 10.1006/bbrc.1996.6046 |
| Citation | Aita N, et al. (1997) Cloning and expression of human liver rhodanese cDNA. Biochem Biophys Res Commun 231(1):56-60 |
| abstractText | 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. |
