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The Formation of N-Glucuronides Catalyzed by Purified Hepatic 17β-Hydroxysteroid and 3α-Hydroxysteroid UDP-Glucuronyltransferases

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Biological Reactive Intermediates III

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 197))

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Abstract

Conjugation of many endogenous and exogenous chemicals with glucuronic acid, catalyzed by UDP-glucuronyltransferases (EC 2.4.1.17), is an important step in their detoxification and elimination from the body. We have previously reported on the purification of three different UDP-glucuronyltransferases (UDPGTs) from hepatic microsomes of female Sprague-Dawley rats1. A 17β-hydroxysteroid UDPGT catalyzes the glucuronidation of the 17β-hydroxy position of steroids, such as testosterone and 17β-estradiol, and xenobiotics such as p-nitrophenol and 1-naphthol. A 3α-hydroxysteroid UDPGT has been purified which is specific for the glucuronidation of the 3α-position of steroids and bile acids2,3. A 3-methylcholanthreneinducible form of p-nitrophenol UDPGT catalyzes the conjugation of various xenobiotic substrates, such as p-nitrophenol, 4-methylumbelliferone and 1-naphthol, with glucuronic acid1.

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© 1986 Plenum Press, New York

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Green, M.D., Irshaid, Y., Tephly, T.R. (1986). The Formation of N-Glucuronides Catalyzed by Purified Hepatic 17β-Hydroxysteroid and 3α-Hydroxysteroid UDP-Glucuronyltransferases. In: Kocsis, J.J., Jollow, D.J., Witmer, C.M., Nelson, J.O., Snyder, R. (eds) Biological Reactive Intermediates III. Advances in Experimental Medicine and Biology, vol 197. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5134-4_38

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  • DOI: https://doi.org/10.1007/978-1-4684-5134-4_38

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5136-8

  • Online ISBN: 978-1-4684-5134-4

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