Purification and Characterization of β-Glucuronidase from Escherichia coli HGU-3,a Human Intestinal Bacterium

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β-Glucuronidase was purified 360-fold from Escherichia coli HGU-3,an human intestinal bacterium. The specific activity of the purified enzyme was 17.78 units/mg protein. The enzyme (M.W. 290000) is composed of four subunits (M.W. 72000) with a pI and optimal pH of 4.8 and 6-7,respectively. The apparent K_m for p-nitrophenyl-β-D-glucuronide was found to be 0.22 mM. The enzyme was inhibited by saccharic acid 1,4-lactone, glycyrrhizin, N-ethylmaleimide (NEM) and p-chloromercuriphenylsulfonic acid (PCMS). Using the bile containing bilirubin diglucuronide as a substrate, the purified β-glucuronidase was able to hydrolyze it to bilirubin. This hydrolyzed bilirubin formed calcium bilirubinate with a reaction mixture containing CaCl_2.
社団法人日本薬学会の論文
1995-09-15