| First Author | Kong AN | Year | 1994 |
| Journal | Chem Biol Interact | Volume | 92 |
| Issue | 1-3 | Pages | 161-8 |
| PubMed ID | 8033251 | Mgi Jnum | J:19853 |
| Mgi Id | MGI:67978 | Doi | 10.1016/0009-2797(94)90061-2 |
| Citation | Kong AN, et al. (1994) Molecular cloning of three sulfotransferase cDNAs from mouse liver. Chem Biol Interact 92(1-3):161-8 |
| abstractText | Sulfate conjugation plays an important role in the biotransformation of not only xenobiotics but also many endogenous substances. Sulfotransferases, the enzymes that are responsible for this process, exist as a superfamily of genes. It has long been recognized that significant species differences exist among drug and carcinogen metabolizing enzymes such as cytochrome P450. Species differences in both regulation and catalytic activities of sulfotransferases may also exist. To investigate this, we conducted cDNA cloning and cDNA expression studies of sulfotransferase in the mouse. Three sulfotransferase cDNA clones were isolated from a female B6CBA mouse liver. Two of the clones, mSTa1 and mSTa2, were highly homologous to each other. Alignment of mSTa1 and mSTa2 cDNAs' nucleotide sequences with those of other sulfotransferase cDNAs revealed the greatest sequence identity with the rat STsmp cDNA. This analysis suggests that mSTa1, mSTa2 and rSTsmp cDNAs are derived from orthologous genes belonging to the alcohol/hydroxysteroid sulfotransferase gene family. The third clone, mSTp1 showed high identity to rSTp, hSTp1, hSTp3, and rSTp1C1, suggesting that mSTp1 belongs to the phenol family. |
