Purification and properties of UDP-glucuronyltransferase from kidney microsomes of beta-naphthoflavone-treated rat

Journal of Biochemistry
H YokotaA Yuasa

Abstract

Rat kidney microsomal UDP-glucuronyltransferase activities toward phenoic xenobiotics were enhanced about 4-5-fold by treatment of the animal with beta-naphthoflavone. The transferase activity toward serotonin, an endogenous substrate, was also enhanced about 7.5-fold. A form of UDP-glucuronyltransferase was purified from kidney microsomes of beta-naphthoflavone-treated rat by solubilization with sodium cholate and two steps of column chromatography, the first with DEAE-Toyopearl (fast flow rate liquid chromatography:FFLC) and the second with UDP-hexanolamine Sepharose 4B (affinity chromatography). These procedures gave about 39-fold purification and 11.5% yield of the transferase activity toward 1-naphthol. The preparation, tentatively termed "GT-2," was highly purified as judged from the single protein band (Mr 54,000) on sodium dodecylsulfate (SDS)-polyacrylamide slab gel electrophoresis. It catalyzed the glucuronidation of not only phenolic xenobiotics such as 1-naphthol, 4-nitrophenol, and 4-methylumbelliferone but also serotonin. From the result that apparent molecular weight of GT-2 was reduced to 50,000 by endo-beta-N-acetylglucosaminidase H (Endo H)-treatment, GT-2 was found to be a 50,000 Da polypeptide carrying "high...Continue Reading

Citations

May 20, 1998·Natural Product Reports·A V Stachulski, G N Jenkins
Dec 18, 2002·Drug Metabolism and Disposition : the Biological Fate of Chemicals·Soundararajan KrishnaswamyMichael H Court
Jun 15, 2007·Toxicological Sciences : an Official Journal of the Society of Toxicology·Junya MatsumotoHiroshi Yokota
Nov 14, 2006·Life Sciences·Nagako TanakaHiroshi Yokota
Sep 22, 2010·Biochemical Pharmacology·M Cristina de AlmagroCarlos J Ciudad

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