Abstract
Summary
Evidences are presented that p-nitrophenol (PNP) and o-aminophenol (OAP) utilize different enzyme systems for their glucuronide conjugation. Included are differences between the two substrates in the kinetics of the reaction, the response to mutual inhibition and to inhibition by a breast-milk inhibitor of bilirubin metabolism, intracellular localization, ability of the responsible enzyme to be solubilized, activity of the conjugating processes in the Gunn rat and in postmortem human liver specimens, and the effects of temperature upon the rate of conjugation. These findings support a concept of multiplicity of UDP-glucuronyl transferase enzymes.
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