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Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC.
We constructed a full-length cDNA coding for 3-methylcholanthrene-inducible rat liver cytochrome P-450MC by the method of Okayama and Berg. The isolated clone pAU157 contained the cDNA insert of 2.7 kb in length. Sequence analysis of the cDNA insert revealed that the amino acid sequence of cytochrome P-450MC was composed of 523 amino acid residues, including the initial 22 N-terminal amino acids whose sequence was determined with the purified protein. The primary structure was found to contain two highly conserved regions as pointed out from comparisons of the reported amino acid sequences of cytochrome P-450 species. The predicted molecular weight of the apoprotein was 59,300 daltons. Therefore, we concluded that the amino acid sequence determined here is for cytochrome P-450MC, probably corresponding to cytochrome P-450c.
PMID: 6324135 [PubMed - indexed for MEDLINE]
PMCID: PMC318716
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Cited by 13 PubMed Central articles
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Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2.
Addya S, Anandatheerthavarada HK, Biswas G, Bhagwat SV, Mullick J, Avadhani NG.
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[J Cell Biol. 1997]
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Distinct organization of methylcholanthrene- and phenobarbital-inducible cytochrome P-450 genes in the rat.
Sogawa K, Gotoh O, Kawajiri K, Fujii-Kuriyama Y.
Proc Natl Acad Sci U S A. 1984 Aug; 81(16):5066-70.
[Proc Natl Acad Sci U S A. 1984]
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Liver mRNA probes disclose two cytochrome P-450 genes duplicated in tandem with the complement C4 loci of the mouse H-2S region.
Amor M, Tosi M, Duponchel C, Steinmetz M, Meo T.
Proc Natl Acad Sci U S A. 1985 Jul; 82(13):4453-7.
[Proc Natl Acad Sci U S A. 1985]
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