Add time:08/20/2019         Source:sciencedirect.com

All-trans-retinoic acid is metabolized in vitro to a biologically active metabolite, retinoyl-β-glucuronide. We have studied the synthesis of this metabolite in vitro. The identity of the product was established by cochromatography on reverse-phase high-performance liquid chromatography, β-d-glucuronidase hydrolysis, and fast atom bombardment and collisionally activated decomposition/fast atom bombardment mass spectrometry. The formation of retinoyl-β-glucuronide is catalyzed by a UDP-glucuronosyltransferase with apparent Km's of 54.7 μm for all-trans-retinoic acid and 2.4 mm for UDP-glucuronic acid. The reaction requires enzyme, UDP-glucuronate, and no other factor. It is strongly inhibited by millimolar concentrations of coenzyme A. The specific activity of UDP-glucuronosyltransferase is greatest in the liver and least in the kidney of those tissues examined. The specific activity of the enzyme is increased by vitamin A deficiency. The increased specific activity observed in the vitamin A-deficient rat liver is uncharacteristic of retinoic acid inactivation enzymes; therefore, retinoyl-β-glucuronide may be of functional importance.

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