| Name | UDPGT |
|---|---|
| Synonyms | UDP glucuronosyltransferase 2B28; UDPGT; UDP glucuronosyltransferase 2B28 precursor; UGT2B28; UDP glucuronosyltransferase 2B28 precursors |
| Name | 1-naphthol |
|---|---|
| CAS | 1-naphthalenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 3101703 | Coughtrie MW, Burchell B, Bend JR: Purification and properties of rat kidney UDP-glucuronosyltransferase. Biochem Pharmacol. 1987 Jan 15;36(2):245-51. Treatment of rats with beta-naphthoflavone resulted in a 3-fold induction of renal UDPGT activity towards 1-naphthol, and and a 2-fold induction of and glucuronidation. |
35(0,1,1,5) | Details |
| 10895755 | Chen TL, Wu CH, Chen TG, Tai YT, Chang HC, Lin CJ: Effects of propofol on functional activities of hepatic and extrahepatic conjugation enzyme systems. Br J Anaesth. 2000 Jun;84(6):771-6. The functional activities of phase-II enzymes, including -glucuronosyltransferase (UDPGT), glutathione S-transferase (GST) and N-acetyltransferase (NAT) were evaluated in the presence of various concentrations of propofol (0.05-1.0 mmol litre-1), using 1-naphthol, 1-chloro-2,4-dinitrobenzene and as substrates respectively. |
34(0,1,1,4) | Details |
| 3128178 | Green MD, Coffman BL, Irshaid YM, Tephly TR: Characterization of antibodies to a rabbit hepatic UDP-glucuronosyltransferase and the identification of an immunologically similar enzyme in human liver. Arch Biochem Biophys. 1988 Apr;262(1):367-74. Sheep anti-rabbit liver PNP UDPGT IgG immunoprecipitated PNP, 1-naphthol, and 4-methylumbelliferone glucuronidation activities in rabbit and human liver microsomal preparations. |
32(0,1,1,2) | Details |
| 7581838 | Zihnioglu F, Telefoncu A: Substrate specificity and the use of -entrapped rabbit hepatic microsomal -glucuronyl transferase for detoxification. Artif Cells Blood Substit Immobil Biotechnol. 1995;23(4):533-43. For studying the drug metabolism in vitro and obtaining artificial liver support (detoxification) -entrapped UDPGT towards 1-naphthol was tested by using two model reactor system. |
31(0,1,1,1) | Details |
| 3085679 | Lilienblum W, Irmscher G, Fusenig NE, Bock KW: Induction of UDP-glucuronyltransferase and arylhydrocarbon hydroxylase activity in mouse skin and in normal and transformed skin cells in culture. Biochem Pharmacol. 1986 May 1;35(9):1517-20. After topical application of Aroclor 1254 to the skin UDPGT activities towards 1-naphthol, 3-hydroxybenzo [a] pyrene and benzo [a] pyrene-7,8-dihydrodiol were increased 3-fold and AHH activity was increased 15-fold. |
15(0,0,2,5) | Details |
| 6416180 | Falany CN, Tephly TR: Separation, purification and characterization of three isoenzymes of UDP-glucuronyltransferase from rat liver microsomes. Arch Biochem Biophys. 1983 Nov;227(1):248-58. Three isoenzymes of UDP-glucuronyltransferase (UDPGT) have been separated and purified from liver microsomes of untreated female rats or female rats pretreated with 3-methylcholanthrene. One isoenzyme exhibits a subunit molecular weight of 56,000 and is capable of conjugating 1-naphthol, and 4-methylumbelliferone. |
6(0,0,0,6) | Details |
| 1631888 | Clarke DJ, Burchell B, George SG: Differential expression and induction of UDP-glucuronosyltransferase isoforms in hepatic and extrahepatic tissues of a fish, Pleuronectes platessa: immunochemical and functional characterization. Toxicol Appl Pharmacol. 1992 Jul;115(1):130-6. Glucuronidation of three substrates prototypical for different UDP-glucuronosyltransferase (UDPGT) isoforms in hepatic, renal, intestinal, and branchial microsomes of corn oil, 3-methylcholanthrene, Aroclor 1254, and clofibrate-pretreated plaice was investigated. |
6(0,0,0,6) | Details |
| 1599427 | Clarke DJ, George SG, Burchell B: Multiplicity of UDP-glucuronosyltransferases in fish. Biochem J. 1992 Jun 1;284 ( Pt 2):417-23. The aim of this work was to determine if a non-mammalian species had multiple UDP-glucuronosyltransferase (UDPGT) isoforms. The purified enzyme conjugated 1-naphthol, but not or steroids, and displayed a pI of 7.0 and a subunit molecular mass of 55 kDa. |
5(0,0,0,5) | Details |
| 2116803 | Miners JO, Lillywhite KJ, Yoovathaworn K, Pongmarutai M, Birkett DJ: Characterization of UDP-glucuronosyltransferase activity in human liver microsomes. Biochem Pharmacol. 1990 Aug 1;40(3):595-600. The procedure has been used to characterize glucuronidation kinetics in human livers microsomes and to assess the substrate specificity of the UDP-glucuronosyltransferase (UDPGT) activity. The glucuronidated xenobiotics chloramphenicol, digitoxigenin monodigitoxoside, 4-hydroxybiphenyl, 4-methylumbelliferone, morphine, 1-naphthol and were screened for inhibitory effects on glucuronidation. |
5(0,0,0,5) | Details |
| 6811722 | Adachi S, Fujita S, Uesugi T: Effect of 1-m-tolueneazo-2-naphthol on hepatic drug metabolism. J Pharmacobiodyn. 1982 Apr;5(4):273-7. Effect of potent cytochrome P-448 inducer, 1-m-tolueneazo-2-naphthol (m-TAN) on hepatic microsomal UDP-glucuronyl-transferase (UDPGT) activity was studied. The UDPGT activities towards 1-naphthol and chloramphenicol were increased up to 6,2.5 and 1.8 folds of control levels respectively, in microsomes from m-TAN treated rats. 3-Methylcholanthrene, on the other hand, caused 4 and 2 fold increase in UDPGT activities towards and 1-naphthol, respectively, but did not cause significant increase in UDPGT activity towards chloramphenicol. |
3(0,0,0,3) | Details |
| 1615704 | Sharp S, Mak LY, Smith DJ, Coughtrie MW: Inhibition of human and rabbit liver steroid and xenobiotic UDP-glucuronosyltransferases by tertiary amine drugs--implications for adverse drug reactions. Xenobiotica. 1992 Jan;22(1):13-25. Chlorpromazine, amitriptyline, promethazine and cyproheptadine were consistently the most potent inhibitors of the glucuronidation of and 1-naphthol, the steroid activities being more susceptible to inhibition (up to 90%). 3. Carbamazepine, sulphadimethoxine, dimenhydrinate and (+/-)- had little effect on the UDPGT activities measured. 4. |
1(0,0,0,1) | Details |
| 1909117 | Tan TM, Wong KP, Sit KH: Expression of a high-affinity form of UDP-glucuronosyltransferase in human foetal liver cells in culture on exposure to mercuric Biochem J. 1991 Aug 15;278 ( Pt 1):99-103. The activity of UDP-glucuronosyltransferase (UDPGT, EC 2.4.1.17) in human foetal liver cells in culture was measured with two acceptor substrates, namely harmol and 1-naphthol. |
5(0,0,0,5) | Details |
| 3143063 | Jackson MR, Fournel-Gigleux S, Harding D, Burchell B: Examination of the substrate specificity of cloned rat kidney UDP-glucuronyltransferase expressed in COS-7 cells. Mol Pharmacol. 1988 Nov;34(5):638-42. A cDNA encoding a rat kidney UDP-glucuronyltransferase (UDPGT) was subcloned into the vector pKCRH2. The expressed enzyme rapidly catalyzed the glucuronidation of 1-naphthol, 4-methylumbelliferone, and |
4(0,0,0,4) | Details |
| 7581839 | Zihnioglu F, Telefoncu A: Preparation and characterization of -entrapped microsomal -glucuronyl transferase. Artif Cells Blood Substit Immobil Biotechnol. 1995;23(4):545-52. Chemical and physical characterization were made by using 1-naphthol as substrate. In conclusion, gel beads appear to have good characteristics for use as UDPGT immobilization support suitable for large scale use and offer the prospect that immobilized UDPGT may become an important form of catalyst in medicine. |
1(0,0,0,1) | Details |
| 7599146 | Zihnioglu F, Telefoncu A: Diffusion characteristics of -entrapped microsomal -glucuronyl transferase gel beads. Biochim Biophys Acta. 1995 Jun 9;1244(2-3):291-4. Rabbit hepatic microsomal -glucuronyl transferase (EC 2.4.1.17) was immobilized by entrapment in which is an ionotropic gelation agent and the resulting preparation was used as a biocatalyst for the glucuronidation of 1-naphthol in order to study the drug metabolism in vitro and obtaining artificial liver support (detoxification). |
0(0,0,0,0) | Details |
| 3240719 | Jagadeesan V, Oesch F: Effects of dietary zinc deficiency on the activity of enzymes associated with phase I and II of drug metabolism in Fischer-344 rats: activities of drug metabolising enzymes in zinc deficiency. Drug Nutr Interact. 1988;5(4):403-13. It was observed that the activities of microsomal epoxide hydrolase (with benz (a) pyrene 4-5 oxide as substrate), diphospho glucuronyl transferase (with 1-naphthol as substrate) and cytosolic glutathione-S-transferase (with chlorodinitrobenzene as substrate) were altered exclusively due to zinc deficiency. |
0(0,0,0,0) | Details |
| 3134892 | Miners JO, Lillywhite KJ, Birkett DJ: In vitro evidence for the involvement of at least two forms of human liver UDP-glucuronosyltransferase in morphine 3-glucuronidation. Biochem Pharmacol. 1988 Jul 15;37(14):2839-45. Chloramphenicol, 4-hydroxybiphenyl, 4-methylumbelliferone, 1-naphthol and were all shown to inhibit the low affinity morphine-UDPGT activity, but only chloramphenicol and 1-naphthol were competitive inhibitors. |
85(1,1,1,5) | Details |
| 1617946 | Clarke DJ, Burchell B, George SG: Functional and immunochemical comparison of hepatic UDP-glucuronosyltransferases in a piscine and a mammalian species. Comp Biochem Physiol B. 1992 Jun;102(2):425-32. Both species exhibited comparable UDP-glucuronosyltransferase (UDPGT) activity towards planar phenolic substrates (1-naphthol, however, plaice activity towards bulky non-planar substrates such as (-)-morphine was either 200-fold lower, or for an arylacetic acid (RS-2-phenylpropionic acid) and an aryloxyacetic acid (clofibric acid) non-detectable. 3. |
81(1,1,1,1) | Details |
| 17178690 | Wolf DC, Allen JW, George MH, Hester SD, Sun G, Moore T, Thai SF, Delker D, Winkfield E, Leavitt S, Nelson G, Roop BC, Jones C, Thibodeaux J, Nesnow S: Toxicity profiles in rats treated with tumorigenic and nontumorigenic triazole conazole fungicides: Propiconazole, triadimefon, and myclobutanil. Toxicol Pathol. 2006;34(7):895-902. diphopho-glucuronosyl transferase (UDPGT), the T4 metabolizing enzyme measured as glucuronidation of 1-naphthol, was induced to the same extent after 30 and 90 days for all three conazoles. |
81(1,1,1,1) | Details |
| 1749222 | Robertson KJ, Clarke D, Sutherland L, Wooster R, Coughtrie MW, Burchell B: Investigation of the molecular basis of the genetic deficiency of UDP-glucuronosyltransferase in Crigler-Najjar syndrome. J Inherit Metab Dis. 1991;14(4):563-79. Analysis of four patient liver samples by immunoblot analysis revealed the heterogeneous nature of this inherited disease within the patient population, and one sample where 1-naphthol UDPGT activity was considerably reduced appeared to correlate with the non-detection of a UDPGT protein. |
81(1,1,1,1) | Details |
| 1804651 | Cappiello M, Giuliani L, Pacifici GM: Distribution of UDP-glucuronosyltransferase and its endogenous substrate 5'-diphosphoglucuronic acid in human tissues. Eur J Clin Pharmacol. 1991;41(4):345-50. The apparent kM for UDPGT depended upon the chemical nature of the UDPGA-acceptor substrate; average values of kM were 63, 300, and 700 mumol.l-1 for 1-naphthol, and morphine respectively. |
40(0,1,2,5) | Details |
| 3096339 | Koster AS, Schirmer G, Bock KW: Immunochemical and functional characterization of UDP-glucuronosyltransferases from rat liver, intestine and kidney. Biochem Pharmacol. 1986 Nov 15;35(22):3971-5. Purification of UDPGT (1-naphthol as substrate) from intestinal microsomes to apparent homogeneity yielded a polypeptide with an apparent molecular weight of 54-56 kDa. |
35(0,1,1,5) | Details |