The separation and purification of rat liver UDP-glucuronyltransferase activities towards testosterone and oestrone

Biochem J. 1980 Aug 1;189(2):377-80. doi: 10.1042/bj1890377.

Abstract

1. Reconstitution of UDP-glucuronyltransferase preparations with phosphataidylcholine liposomes facilitated the purification of testosterone UDP-glucuronyltransferase. 2. Transferase activity towards testosterone co-purifies with that towards 4-nitrophenol. 3. UDP-glucuronyltransferase activity towards oestrone was separated from that towards testosterone. 4. These results suggest that testosterone and 4-nitrophenol may be glucuronidated by a different form of UDP-glucuronyltransferase from the one glucuronidating oestrone.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chromatography, DEAE-Cellulose
  • Estrone
  • Glucuronosyltransferase / isolation & purification*
  • Glucuronosyltransferase / metabolism
  • Liposomes
  • Liver / enzymology*
  • Methods
  • Nitrophenols
  • Phosphatidylcholines
  • Rats
  • Testosterone

Substances

  • Liposomes
  • Nitrophenols
  • Phosphatidylcholines
  • Estrone
  • Testosterone
  • Glucuronosyltransferase