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Automation of a Luminescent Assay to measure UDP-glucuronosyltransferase (UGT) Enzyme Activity

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Related Products: Precision

September 11, 2009

 

Authors: Brad Larson, Peter Banks, BioTek Instruments, Inc.; Jessica Anderson, James Cali, Promega Corporation

 

 

 

Abstract

 

The UDP-glucuronosyltransferase (UGT) enzyme is responsible for the catalyzation of the glucuronidation reaction. This reaction involves the transfer of a hydrophilic glucuronysyl group from uridine 5’-diphospho-glucuronic acid (UDPGA) to a substrate. Through this function, the UGT enzyme family plays an important role in the elimination of drugs and other chemicals from the body. This has caused an increased interest in the study of how altered UGT function can contribute to potential drug-drug interactions in the body.

Here we demonstrate the automation of a 384-well luminescent assay which incorporates pro-luminogenic substrates to assess UGT activity. Automation consists of an inexpensive pipetting station to perform serial dilution of compounds to be tested as well as low volume reagent addition. Z’-Factor values, as well as pharmacology confirm that this combination of assay and instrumentation provides an easy to use, robust solution for automated UGT enzyme profiling.

 

 

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