| First Author | Ohgiya S | Year | 1994 |
| Journal | Biochim Biophys Acta | Volume | 1186 |
| Issue | 1-2 | Pages | 137-41 |
| PubMed ID | 8011664 | Mgi Jnum | J:19597 |
| Mgi Id | MGI:67742 | Doi | 10.1016/0005-2728(94)90146-5 |
| Citation | Ohgiya S, et al. (1994) Mouse NADPH-cytochrome P-450 oxidoreductase: molecular cloning and functional expression in yeast. Biochim Biophys Acta 1186(1-2):137-41 |
| abstractText | We published isolation of a mouse NADPH-cytochrome P-450 oxidoreductase cDNA and afterward ascribed the cDNA to the guinea-pig instead of the mouse (Ohgiya, S. et al. (1992) Biochim. Biophys. Acta 1171, 103-105 and Corrigendum (1993) Biochim. Biophys. Acta 1174, 313). We report here nucleotide and deduced amino acid sequences of an NADPH-cytochrome P-450 oxidoreductase cDNA isolated from the ddY mouse. The mouse cytochrome P-450 oxidoreductase shares 98.4% identity with its rat counterpart. In particular, clusters of acidic residues that presumably participate in interaction with cytochrome P-450 are highly conserved in primary structures of mammalian cytochrome P-450 oxidoreductases. The mouse cytochrome P-450 oxidoreductase was functionally expressed in yeast using a modified cDNA clone lacking whole noncoding regions. |
