Purification of cytochrome P-450 from polychlorinated biphenyl-treated crab-eating monkeys: high homology to a form of human cytochrome P-450.
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.
Ohta
K
K
Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Kitada
M
M
Hashizume
T
T
Komori
M
M
Ohi
H
H
Kamataki
T
T
D000595:Amino Acid Sequence; D000818:Animals; D000937:Antigen-Antibody Reactions; D001711:Biotransformation; D003577:Cytochrome P-450 Enzyme System / Q000302:isolation & purification*; D008251:Macaca / Q000502:physiology*; D008252:Macaca fascicularis / Q000502:physiology*; D008862:Microsomes, Liver / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011078:Polychlorinated Biphenyls / Q000494:pharmacology
D003577:Cytochrome P-450 Enzyme System; D011078:Polychlorinated Biphenyls