β-Glucuronidases are hydrolytic enzymes responsible for the breakdown of carbohydrates.  Specifically, β-Glucuronidases cleave the terminal β-D-glucuronic acid residue from the non-reducing terminus of a mucopolysaccharide chain.  In humans, these enzymes are found in the lysosome of many tissue types.  Loss of β-Glucuronidase activity results in a metabolic disease known as Sly syndrome.  One pharmaceutical application for these enzymes is the metabolism of glucuronidated prodrugs into active pharmacological compounds.  As expression and activities of β-Glucuronidases vary substantially between tissue types and disease states, these enzymes have been used to achieve targeted activation of oncotherapeutic compounds, some of which may be toxic to healthy cells not associated with malignancy or disease.  It is thus important to have knowledge of the β-Glucuronidase activity in the tested sample to determine whether the prodrug or active form will predominate.