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Attempts to phenotype human liver samples in vitro for debrisoquine 4‐ hydroxylase activity.
Author(s) -
Boobis AR,
Hampden CE,
Murray S,
Beaune P,
Davies DS
Publication year - 1985
Publication title -
british journal of clinical pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.216
H-Index - 146
eISSN - 1365-2125
pISSN - 0306-5251
DOI - 10.1111/j.1365-2125.1985.tb02706.x
Subject(s) - debrisoquine , hydroxylation , cytochrome p450 , phenotype , in vitro , cytochrome , enzyme , biochemistry , biology , in vivo , chemistry , pharmacology , cyp2d6 , genetics , gene
Twenty‐eight samples of human liver have been characterised for cytochrome P‐450 content, aldrin epoxidase, debrisoquine 4‐hydroxylase and bufuralol 1'‐hydroxylase activities. Evidence is presented here and elsewhere that bufuralol 1'‐hydroxylase and debrisoquine 4‐hydroxylase are activities catalysed by the same form of cytochrome P‐450 in man, and that this form is different from that catalysing the epoxidation of aldrin. Attempts to phenotype liver samples in vitro, in the absence of any metabolic data in vivo for debrisoquine 4‐hydroxylation status, met with limited success. A combination of enzyme assays will most probably be required in any such phenotyping of human liver samples.