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 |
|---|---|
| Pages (from-to) | 69-75 |
| Number of pages | 7 |
| Journal | Journal of biochemistry |
| Volume | 88 |
| Issue number | 1 |
| Publication status | Published - Jul 1 1980 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
Cite this
Studies on the αL-iduronidase activity of β-glucuronidase preparations from bovine liver, rat liver, and rat preputial gland. / Kosaka, Hiroko; Isemura, Mamoru; Ono, Teruo; Nishimura, Yukio; Kato, Keitaro.
In: Journal of biochemistry, Vol. 88, No. 1, 01.07.1980, p. 69-75.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Studies on the αL-iduronidase activity of β-glucuronidase preparations from bovine liver, rat liver, and rat preputial gland
AU - Kosaka, Hiroko
AU - Isemura, Mamoru
AU - Ono, Teruo
AU - Nishimura, Yukio
AU - Kato, Keitaro
PY - 1980/7/1
Y1 - 1980/7/1
N2 - 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.
AB - 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.
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M3 - Article
VL - 88
SP - 69
EP - 75
JO - Journal of Biochemistry
JF - Journal of Biochemistry
SN - 0021-924X
IS - 1
ER -