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 language | English |
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Pages (from-to) | 1097-1102 |
Number of pages | 6 |
Journal | Journal of Steroid Biochemistry |
Volume | 19 |
Issue number | 2 |
DOIs | |
Publication status | Published - Aug 1983 |
Externally published | Yes |