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The Effects of Lipid-Protein Interactions on the Kinetic Parameters of Microsomal UDP-Glucuronyltransferase

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Book cover The Enzymes of Bioligical Membranes

Abstract

The study of glucuronidation reactions began 100 years ago with the isolation of a conjugate of o-nitrotoluene from the urine of dogs. Acid hydrolysis of this conjugate yielded an acidic sugar as one of the products. An identical sugar was obtained on acid hydrolysis of a conjugate of chloral hydrate exreted in human urine. The formula of the reducing sugar was given correctly as

$$ {\left( {{\rm{CHOH}}} \right)_4}\left\{ {\begin{array}{*{20}{c}} {{\rm{CHO}}}\\ {{\rm{COOH}}} \end{array}} \right. $$

by Schmiedeberg and Meyer in 1879 (Smith and Williams, 1970). A wide variety of organic compounds are now known to be conjugated with glucuronic acid. Predominant among these are aromatic molecules containing phenolic and carboxylic groups which form O-ether and O-ester glucuronides, respectively. Several aromatic thiols are glucuronidated, and N-glucuronides also have been reported (Dutton, 1966). The donor of the glucuronic acid moiety in these reactions was identified as UDP-glucuronic acid (Dutton and Storey, 1953; Dutton, 1966).

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Zakim, D., Vessey, D.A. (1976). The Effects of Lipid-Protein Interactions on the Kinetic Parameters of Microsomal UDP-Glucuronyltransferase. In: Martonosi, A. (eds) The Enzymes of Bioligical Membranes. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-2655-7_12

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