Solid-phase synthesis and drug glucuronides by immobilized glucuronosyltransferase

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Abstract
Rabbit liver glucuronosyltransferase immobilized on beaded agarose was used to synthesize glucuronic acid conjugates of meprobamate, diethylstilbestrol, bilirubin, borneol, benzoic acid and p-nitrothiophenol. The immobilized enzyme exhibited a high degree of specificity for UDPGA [UDP-glucuronic acid] as cofactor when p-nitrophenol is used as a substrate. Other cofactors tested were less effective, all producing less than 10% conjugation relative to UDPGA. The effects on agarose-bound enzyme activity of a variety of cosolvents and emulsifiers were studied. Ethanol, dimethyl sulfoxide, propylene glycol and bovine serum albumin are among the cosolvents and emulsifiers which can be used within limited concentration ranges to solubilize lipophilic substrates for conjugation. Concentrations of Ca and Mg between 1.5 and 10.0 mM enhanced glucuronosyltransferase activity of the immobilized enzyme.

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