| First Author | Tomita Y | Year | 1977 |
| Journal | J Dermatol | Volume | 4 |
| Issue | 6 | Pages | 245-9 |
| PubMed ID | 15461355 | Mgi Jnum | J:93371 |
| Mgi Id | MGI:3056952 | Doi | 10.1111/j.1346-8138.1977.tb00994.x |
| Citation | Tomita Y, et al. (1977) Inactivation mechanism of tyrosinase in mouse melanoma. J Dermatol 4(6):245-9 |
| abstractText | Tyrosinase [EC 1.14.18.1] isolated from mouse melanoma was inactivated during the dopa-tyrosinase reaction. When ascorbate was added to the reaction system, in which dopa-quinone is immediately converted back to dopa by ascorbate thus preventing the formation of melanin, tyrosinase inactivation similarly occurred. If superoxide anions (O2-) or singlet oxygens (1O2), are generated during the reaction they can attack the enzyme protein to be inactivated. Therefore an estimate was made with scavengers for oxygen radicals and with a liquid scintillation counter but neither was detectable. Thus the inactivation involved is not due to reaction products nor oxygen |
