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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Glucuronidation of diflunisal by rat liver microsomes. Effect of microsomal beta-glucuronidase activity.

The in vitro formation rates of the phenolic (DPG) and acyl ( DAG) glucuronides of diflunisal were investigated using rat liver microsomes. Preliminary studies showed that DAG hydrolysed rapidly (T1/2 = 12 min) when incubated in the presence of rat liver microsomes at pH 7.4 and 37 degrees. DPG was much more stable under the same conditions (T1/2 = 35 hr). Hydrolysis of DAG and DPG by rat liver microsomes was inhibited by 4 mM saccharolactone, a beta-glucuronidase inhibitor. The apparent Km and Vmax values for the formation of DAG in the absence and presence of 4 mM D-saccharic acid-1,4-lactone (saccharolactone) were the following: Km = 0.05 +/- 0.02 vs 0.08 +/- 0.02 mM and Vmax = 0.20 +/- 0.06 vs 0.43 +/- 0.07 nmol/min/mg protein (0 and 4 mM saccharolactone, respectively). The significant increase in apparent Vmax for DAG formation in the presence of saccharolactone can be explained by the inhibition of beta-glucuronidase-catalysed hydrolysis of DAG. Apparent Km and Vmax values for the formation rate of DPG were not affected by addition of saccharolactone to the incubation medium. These results indicate that beta-glucuronidase-catalysed hydrolysis of certain glucuronides formed during microsomal incubations may significantly affect the apparent glucuronidation rate due to the presence of a glucuronidation-deglucuronidation cycle.[1]


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