Ox spleen β-glucuronidase; its purification and a study of some factors involved in assaying its activity

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Abstract
[beta]-glucuronidase from ox-spleen was purified by isoelectric precipitation of inactive protein followed by (NH4)2SO4 fractionation at pH 4.3, 5.0, and 7.3. The purified enzyme was specific for [beta]-glucuronides, not hy-drolyzing phenyl-[beta]-glucoside, salicin, or cellobiose. Aqueous extracts of acetone treated ox-spleen liberated large amts. of dialyzable reducing material when incubated at 25 [degree] at pH 5.0; the process being complete after 6-8 hrs. whereby the enzyme activity was increased 100%. A iS-glucuronidajsie unit (G. U.) was defined as the amt. of enzyme which liberated 0.1 mg. glucuronic acid from 1-menthol glucuronide under specified conditions.

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