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Hydroxylation of desmethylimipramine: Dependence on the debrisoquin hydroxylation phenotype
Author(s) -
Spina Edoardo,
Steiner Eugen,
Ericsson Örjan,
Sjöqvist Folke
Publication year - 1987
Publication title -
clinical pharmacology and therapeutics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.941
H-Index - 188
eISSN - 1532-6535
pISSN - 0009-9236
DOI - 10.1038/clpt.1987.33
Subject(s) - hydroxylation , chemistry , pharmacology , clinical pharmacology , debrisoquine , enzyme , medicine , endocrinology , biology , cyp2d6 , biochemistry , cytochrome p450
The 2‐hydroxylation of desmethylimipramine (DMI) was studied in 14 healthy subjects previously phenotyped with respect to debrisoquin hydroxylation. After a single oral dose (25 mg), slow hydroxylators of debrisoquin had significantly lower total and metabolic clearances and longer plasma half‐lives of DMI and excreted less 2‐hydroxydesmethylimipramine than did rapid hydroxylators. These findings strengthen the hypothesis that the hydroxylations of debrisoquin and DMI may be under common enzymatic control. Clinical Pharmacology and Therapeutics (1987) 41, 314–319; doi: 10.1038/clpt.1987.33