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  • Journal
    Digital Access
    Provider
    Version
    Wiley
    v. 1-, 1982-
    PubMed Central
    v. 1-, 1982- Full text delayed 12 months
    Print Access Request
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    Stored offsite. Please request print.
    v. 1-22, 1982-2003.
    169
  • Article
    Ali SS, Elliott WH.
    Biochim Biophys Acta. 1975 Nov 21;409(2):249-57.
    Rabbit liver microsomal preparations fortified with 0.1 mM NADPH effectively promote hydroxylation of [3beta-3H]- or [24-14C]allochenodeoxycholic acid or [5alpha,6alpha-3H2]5alpha-cholestane-3alpha,7alpha-diol to their respective 12alpha-hydroxyl derivatives in yields of about 25 or 65% in 60 min. Minor amounts of other products are formed from the diol. The requirements for activity of rabbit liver microsomal 12alpha-hydroxylase resemble those of rat liver microsomes. Of a number of enzyme inhibitors studied only p-chloromercuribenzoate demonstrated a marked ability to inhibit the reaction with either tritiated substrate. There was no difference in the quantity of product produced from the tritiated acid or the 14C-labeled acid. No clear sex difference was found in activity of the enzyme, nor was an appreciable difference noted in activity of the enzyme between mature and immature animals.
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