Miura T, Muraoka S, Ogiso T
Department of Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru, Japan.
Biochem Mol Biol Int. 1995 Jul;36(3):587-94.
The effect of ferrylmyoglobin (ferrylMb) on proteins and its inducement of protein damage is shown, using bovine serum albumin (BSA) as the protein. Oxidation of sulfhydryl (SH) groups of BSA, cross-linking of BSA with myoglobin and inactivation of SH enzymes by ferrylMb were investigated. Our results have shown that ferrylMb rapidly oxidates BSA but failed to oxidate N-ethylmaleimide-treated BSA. During the reaction ferrylMb was reduced to metmyoglobin (metMb) by BSA, myoglobin-binding BSA was formed, and there was a rapid loss of SH enzyme inactivity.
