The transport of glucuronides synthesized in the luminal compartment of the endoplasmic reticulum by UDP-glucuronosyltransferase isoenzymes was studied in rat liver microsomal vesicles. Microsomal vesicles were loaded with p-nitrophenol glucuronide (5 mM), phenolphthalein glucuronide or UDP-glucuronic acid, by a freeze-thawing method. In was shown that: (i) the loading procedure resulted in mil...

Microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone has been isolated from rat liver and appears to be homogeneous in sodium dodecyl sulfate gel electrophoresis and polyacrylamide gradient gel electrophoresis. The conjugating activities toward chenodeoxycholic acid and testosterone co-purified and showed identical mobilities in disc gel electrophoresis,...

To investigate the mechanism for the enhanced glucuronidation of valproic acid (VPA) by panipenem (PAPM), a carbapenem antibiotic, in rat liver, we carried out studies to investigate whether PAPM increases the activity of UDP-glucuronosyltransferase or the level of hepatic UDP-glucuronic acid (UDPGA) in rats. PAPM had no effect on the UDP-glucuronosyltransferase activity toward VPA both in vivo...

Microsomal UDP-glucuronosyltransferase activity toward chenodeoxycholic acid and testosterone has been isolated from rat liver and appears to be homogeneous in sodium dodecyl sulfate gel electrophoresis and polyacrylamide gradient gel electrophoresis. The conjugating activities toward chenodeoxycholic acid and testosterone co-purified and showed identical mobilities in disc gel electrophoresis,...

UDP-glucuronosyltransferase 1A1 (UGT1A1) is a vital metabolic enzyme responsible for the clearance of endogenous substances and drugs. Hitherto, development fluorescent probes UGTs was severely restricted due to poor isoform selectivity on–off or blue-shifted fluorescence response. Herein, we established novel “molecular-splicing” strategy construct highly selective near-infrared (NIR) probe, H...

Brady, R. O., Kanfer, J. N. & Shapiro, D. (1965) Biochem. Biophys. Res. Commun. 18,221-225 Brady, R. O., Pentchev, P. G., Gal, A. E., Hibbert, S. R. & Dekaban, A. S. (1974) N. Engl. J. Med. 291,989-993 Gregoriadis, G. (1974) in Enzyme Replacement Therapy of Lysosomal Storage Diseases (Tager, J. M., Hooghwinke1.G. J. M. &Daems, W. Th.,eds.),pp. 131-148,North-Holland Publishing Co., Amsterdam and...