β-Glucuronidase is a widely distributed enzyme which acts in acid pH optimum to hydrolyze the β-glycosidic bond between glucuronic acid and a variety of other moieties, including steroids, many hydroxylated aromatic compounds, and sugar derivatives. Its activities are particularly high in reproductive organs,1 circulating leukocytes,2,3 and activated macrophages4 as well as in epithelial tissues in general. Proposed natural substrates include the glucuronide conjugates of estrogens and other steroidal hormones and the oligosaccharide products of mucopolysaccharide degradation.1 In most tissues, the enzyme exists predominantly in a latent form, distributing with lysosomes and microsomes.5 From this bound state, it may be released into a free or non-sedimentable form during the process of autolysis,6 ischemic necrosis,7 bacterial or traumatic shock,8 experimental muscular dystrophy,9 and vitamin A intoxication.10 In relation to the neoplastic process, most, but not all, human and experimental tumors show
ALLEN N, REAGAN E. β-Glucuronidase Activities in Cerebrospinal Fluid. Arch Neurol. 1964;11(2):144–154. doi:10.1001/archneur.1964.00460200040004
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