Human cytochrome P450 1B1 (CYP1B1) is found mainly in extrahepatic tissues and is overexpressed in a array of animal tumors. Metabolic activation of 17β-estradiol (E2) to 4-hydroxy E2 by CYP1B1 has been accepted to be an important agency in mammary carcinogenesis. The inhibition of recombinant animal CYP1B1 by 2,2′,4,6′-tetramethoxystilbene (TMS) was advised application either the Escherichia coli membranes of recombinant animal CYP1B1 coexpressed with animal NADPH-P450 reductase or application antiseptic enzyme. 2,2′,4,6′-TMS showed almighty and careful inhibition of ethoxyresorufin O-deethylation (EROD) action of CYP1B1 with IC50 ethics of 2 nM. 2,2′,4,6′-TMS apparent 175-fold selectivity for CYP1B1 over CYP1A1 (IC50, 350 nM) and 85-fold selectivity for CYP1B1 over CYP1A2 (IC50, 170 nM). However, inhibition of animal NADPH-P450 reductase action by 2,2′,4,6′-TMS was negligible. The modes of inhibition by 2,2′,4,6′-TMS were noncompetitive for CYP1A1 and CYP1B1.
More about: Cytochrome P450 1B1 (human) Yeast Reductase sale
Read more: Medicine raw materials
No comments:
Post a Comment