作者: C R Geren , L M Geren , K E Ebner
DOI: 10.1016/S0021-9258(18)71869-3
关键词: Biochemistry 、 Uridine diphosphate galactose 、 NAD+ kinase 、 Uracil nucleotide 、 Carbohydrate Epimerases 、 Chemistry 、 Uridine diphosphate glucose 、 Uridine 、 Enzyme 、 Glycerol-3-phosphate dehydrogenase 、 Molecular biology
摘要: Bovine liver and mammary UDP-galactose-4-epimerases were investigated with respect to various inhibitors inactivators. Uridine nucleotides NADH are potent Ki values in the low micromolar range. The NAD+/NADH ratio may be an important physiological control mechanism for it affects markedly activity of enzyme 50% inhibition occurring at a 20:1. In presence uridine binding epimerases is enhanced. Consequently, effect changes vivo would not immediately apparent as slow down displacement by NAD+. Neither nor galactose 1-phosphate inhibits purified enzymes previously reported impure enzyme. provide almost total protection against first order inactivation trypsin allow determination dissociation constants. NAD+ partially protects inactivation. Inactivation sulfhydryl reagents complex results indicate that least three groups modified before occurs. Partial occurs upon modification 2-hydroxy-5-nitrogenzyl bromide. Some this provided combination UDP.