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beta-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 Km for p-nitrophenyl-beta-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 beta-glucuronidase was able to hydrolyze it to bilirubin. This hydrolyzed bilirubin formed calcium bilirubinate with a reaction mixture containing CaCl2.
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Y H Jin, and
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M J Han, and
K Kobashi
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Protein expression and purification,
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K Kobashi
July 2005,
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D H Kim, and
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D H Kim, and
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D H Kim, and
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