Purification and characterization of human liver cytochrome P-450-ALC.
作者： Jerome M. Lasker , Judy Raucy , Shinji Kubota , Barbara P. Bloswick , Martin Black
DOI: 10.1016/0006-291X(87)91100-4
关键词:
摘要: Abstract Cytochrome P-450-ALC, an ethanol-oxidizing form of microsomal cytochrome P-450 (P-450), has been purified from human liver. P-450-ALC (Mr = 54,000 daltons) is a low-spin ferric hemeprotein with CO-reduced Soret maximum at 452 nm, and NH2-terminal amino acid sequence nearly identical to that deduced cDNA clone. In reconstituted system, oxidizes ethanol aniline turnover rates (12.2 7.3 nmol min−1, respectively) 10-fold greater than two other isozymes (termed P-450-B P-450-C) the same Both P-450-C effectively demethylate N-nitrosodimethylamine (NDMA) low substrate concentrations (0.5 mM), especially in presence b5. Our results provide direct evidence for liver isozyme humans catalytic properties similar related alcohol-inducible rodent P-450s also reveal new NDMA demethylase.
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