Abstract
The partition coefficients between octanol and pH 7.4 buffer for eleven substrates of UDP-glucuronosyltransferase (EC 2.4.1.17) have been determined. They range between 1.1 and 690 in the order p-aminophenol < phenol < ( o-aminobenzoic acid = o-aminophenol = p-aminobenzoic acid) < p-nitrophenol < 4-methylumbelliferone < mercaptobenzothiazole < harmol < phenolphthalein < 1-naphthol. The effect of Triton X-100, used as a model membrane pertubant, on the enzyme activity of UDP-glucuronosyltransferase in rat liver homogenates towards these substrates was determined and compared with the partition coefficients. Enzyme activities towards p-aminophenol and phenol were decreased by Triton X-100, the enzyme activities towards other acceptor substrates were enhanced maximally with 0.025% (w/v) Triton. ‘Native’ enzyme activity (except for amino containing compounds) and activation could be related to partition coefficient of the substrate. An increase in lipid solubility resulted in reduced enzyme activity in untreated homogenates and greater activation. These results suggest UDP-glucuronosyltransferase lies behind a partially lipid-impenetrable barrier and it is suggested that this barrier is broken up by membrane perturbants to permit free access of the more lipid-soluble substrates. In addition, the formation in vitro of a glucuronide from mercaptobenzothiazole was demonstrated.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
