Identification of the human liver cytochrome P-450 responsible for coumarin 7-hydroxylase activity

J. S. Miles, A. W. McLaren, L. M. Forrester, M. J. Glancey, M. A. Lang, C. R. Wolf

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    209 Citations (Scopus)

    Abstract

    1. We have constructed a full-length human liver cytochrome P450IIA cDNA from a partial-length clone by oligonucleotide-directed mutagenesis, and subcloned it into the monkey kidney (COS-7) cell expression vector, pSVL. 2. The cDNA encodes a 49 kDa protein with coumarin 7-hydroxylase (COH) activity which cross-reacts with antisera to the mouse cytochrome P-450 isoenzyme responsible for COH activity and comigrates with a human liver microsomal protein. 3. Western blot analysis of a panel of human livers indicates that the level of the 40 kDa protein, detected using antisera to either the mouse COH P-450 or rat P450IIA1 protein, correlates very highly with COH activity. 4. Antisera to the rat P450IIA1 protein can inhibit COH activity in human liver microsomes. Taken together, these data indicate that a member of the P450IIA subfamily is responsible for most, if not all, of the COH activity in human liver.

    Original languageEnglish
    Pages (from-to)365-371
    Number of pages7
    JournalBiochemical Journal
    Volume267
    Issue number2
    DOIs
    Publication statusPublished - 15 Apr 1990

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

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