title: Purification and characterization of bilirubin UDP-glucuronyltransferase from the liver of eel, Anguilla japonica.
abstract: 1. The enzyme bilirubin uridine diphosphate glucuronyltransferase (UDPGT) was purified and characterized from the liver of eel, Anguilla japonica. 2. The molecular weight of the enzyme was 88,000. 3. The optimal working pH of the enzyme was 7.5-8.0. The optimal working temperature of the enzyme was around 46 degrees C. 4. The Km of bilirubin and uridine diphosphate glucuronic acid for this enzyme was 1.6 mM and 1.8 mM respectively. 5. The concentration of bilirubin did not show any significant effect of inhibition on this enzyme up to 3.3 mM. 6. Since this is the first time UDPGT has been purified and characterized from poikilothermic aquatic animals, it provided interesting information on evolution and adaptation of this enzyme when compared to that of mammals.
authors.affiliation: Department of Marine Resources, National Sun Yat-sen University, Kaohsiung, Taiwan, Republic of China.
authors.forename: L S
authors.initials: LS
authors.lastname: Fang
authors.forename: M S
authors.initials: MS
authors.lastname: Hung
mesh_terms: D000811:Anguilla / Q000378:metabolism*; D000818:Animals; D001663:Bilirubin / Q000378:metabolism*; D014453:Glucuronosyltransferase / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D013696:Temperature
chemical_list: D014453:Glucuronosyltransferase; D001663:Bilirubin