Abstract
A commercial preparation of bovine liver β-glucuronidase contained two distinct enzyme species, both of which catalyze the hydrolysis of 4-methylumbelliferyl α-L-iduronide. The species with a molecular weight of about 290,000 was devoid of phenyl α-L-iduronidase activity and exhibited 4-methylumbelliferyl β-D-glucuronidase activity. The species with a molecular weight of about 78,000 was active towards phenyl α-L-iduronide but lacked the latter activity. Studies of the kinetics of inhibition and heat inactivation suggested that the hydrolysis of 4-methylumbelliferyl α-L-iduronide is due to the β-glucuronidase in the case of the 290,000-dalton species. The highly purified β-glucuronidase preparations derived from rat preputial gland and liver lysosomes also exhibited 4-methylumbelliferyl α-L-iduronidase activity. These findings support the view that β-glucuronidase can hydrolyze certain α-L-iduronide bonds and raise the possibility that β-glucuronidase may play a role in the catabolism of iduronic acid-containing glycosaminoglycans.
Original language | English |
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Pages (from-to) | 69-75 |
Number of pages | 7 |
Journal | Journal of biochemistry |
Volume | 88 |
Issue number | 1 |
Publication status | Published - Jul 1 1980 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology