Ohta K, Kitada M, Hashizume T, Komori M, Ohi H, Kamataki T
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Biochim Biophys Acta. 1989 Jun 13;996(1-2):142-5. doi: 10.1016/0167-4838(89)90107-6.
Cytochrome P-450, designated as P-450-MK2, was purified to an electrophoretic homogeneity from polychlorinated biphenyl (PCB)-treated female crab-eating monkeys. P-450-MK2 catalyzed nifedipine and nilvadipine oxidations, at a rate comparable to human P-450-HM1. The N-terminal amino acid sequence of P-450-MK2 was highly homologous to those of P-450-HM1 and NF 25. The antibodies to P-450-HM1 recognized P-450-MK2 and effectively inhibited the activity of testosterone 6 beta-hydroxylase in monkey liver microsomes. These results suggest that a form of cytochrome P-450 corresponding to human P-450-HM1 or P-450NF which belongs to the P450 III gene family is also present in liver microsomes of crab-eating monkeys.
