Purification of a form of mouse liver UDP glucuronosyltransferase which glucuronidates androgens

Peter I. Mackenzie, Ida S. Owens

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

A form of UDP glucuronosyltransferase active in the glucuronidation of the androgens, testosterone, androsterone and dihydrotestosterone has been purified to apparent homogeneity as judged by sodium dodecylsulfate polyacrylamide gel electrophoresis from the livers of phenobarbital-treated C57BL/6N mice. This UDP glucuronosyltransferase is inactive towards estrone as substrate. Data from chromatofocusing and purification experiments suggest that testosterone and androsterone are glucuronidated primarily by this enzyme form and to a lesser extent by an enzyme form which has a slightly higher isoelectric point. However, this major form is only responsible for about half the capacity to glucuronidate dihydrotestosterone.

Original languageEnglish
Pages (from-to)1097-1102
Number of pages6
JournalJournal of Steroid Biochemistry
Volume19
Issue number2
DOIs
Publication statusPublished - Aug 1983
Externally publishedYes

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