Purification and Characterization of a Morphine UDP-Glucuronyltransferase Isoform from Untreated Rat Liver

Yuji Ishii, Kazuta Oguri, Hidetoshi Yoshimura

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11 Citations (Scopus)

Abstract

A morphine UDP-glucuronyltransferase was purified from liver microsomes of untreated Sprague-Dawley rats. A new gel, ω-(β-carboxypropionylamino)octyl Sepharose 4B, was prepared by coupling monomethylsuccinate with ω)-aminooctyl Sepharose 4B and this was used as an efficient tool for the separation of microsomal enzymes. Emulgen 911 solubilized microsomes were applied to a column packed with the gel and eluted at pH 7.4 while increasing KCl concentration in a stepwise manner. An isoform was further purified with UDP-hexanolamine Sepharose 4B gel. The purified UDP-glucuronyltransferase (morphine UGT of untreated rat, morphine UGTut) exhibited a molecular weight of 52000 on sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and was capable of glucuronidating the 3-hydroxyl group of morphine. The isoform catalyzed to a small extent the glucuronidation of 4-hydroxybiphenyl; however, no glucuronidation activity towards androsterone, testosterone, bilirubin, 4-nitrophenol and the 6-hydroxyl group of morphine was observed. The difference in properties, compared with morphine UGT (molecular weight 56000) which was purified previously from phenobarbital-treated rats, is discussed.

Original languageEnglish
Pages (from-to)754-758
Number of pages5
JournalBiological and Pharmaceutical Bulletin
Volume16
Issue number8
DOIs
Publication statusPublished - Jan 1 1993

All Science Journal Classification (ASJC) codes

  • Pharmacology
  • Pharmaceutical Science

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