STUDIES ON THE ALPHA-L-IDURONIDASE ACTIVITY OF BETA-GLUCURONIDASE PREPARATIONS FROM BOVINE LIVER, RAT-LIVER, AND RAT PREPUTIAL GLAND

  • 1 January 1980
    • journal article
    • research article
    • Vol. 88  (1) , 69-75
Abstract
A commercial preparation of bovine liver .beta.-glucuronidase contained 2 distinct enzyme species, both of which catalyze the hydrolysis of 4-methylumbelliferyl .alpha.-L-iduronide. The species with a MW of about 290,000 was devoid of phenyl .alpha.-L-iduronidase activity and exhibited 4-methylumbelliferyl .beta.-D-glucuronidase activity. The species with a MW of about 78,000 was active towards phenyl .alpha.-L-iduronide but lacked the latter activity. Studies of the kinetics of inhibition and heat inactivation suggested that the hydrolysis of 4-methylumbelliferyl .alpha.-L-iduronide is due to the .beta.-glucuronidase in the case of the 290,000-dalton species. The highly purified .beta.-glucuronidase preparations derived from rat preputial gland and liver lysosomes exhibited 4-methylumbelliferyl .alpha.-L-iduronidase activity. .beta.-Glucuronidase can apparently hydrolyze certain .alpha.-L-iduronide bonds and may play a role in the catabolism of iduronic acid-containing glycosaminoglycans.

This publication has 0 references indexed in Scilit: