Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Characterization of ethanol-inducible human liver N-nitrosodimethylamine demethylase

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00370a001· OSTI ID:6592537
Through the use of monospecific antibodies directed against hepatic cytochrome P-450j, an enzyme induced in rats treated with ethanol or isoniazid, we have purified from human liver the related cytochrome P-450 termed HLj. HLj resembles rat P-450j and P-450 LM3a, the homologous cytochrome in rabbit liver, in its NH/sub 2/-terminal amino acid sequence, in being in highest concentration in liver microsome samples prepared from two patients intoxicated by ethanol and one patient given isoniazid, and in catalyzing the metabolic activation of the procarcinogen N-nitrosodimethylamine. Furthermore, each of nine human liver RNA samples contained a species of mRNA hybridizable to a cloned HLj cDNA. We conclude that HLj is related by structure, function, and some regulator characteristics to rat P-450j and rabbit P-450 LM3a, cytochromes critical for metabolism of several clinically relevant cytotoxic and carcinogenic agents.
Research Organization:
Medical College of Virginia, Richmond
OSTI ID:
6592537
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 25:22; ISSN BICHA
Country of Publication:
United States
Language:
English