Abstract
In the phenolphthalein mono-β-glucuronide method for β-glucuronidase assay, diminished enzyme levels have been observed when trichloroacetic acid or heat coagulation are used for deproteinization, but not when acetone is used for this purpose. Data are presented to show the effect of these reagents when blood serum is used as a source of enzyme. The optimum pH of serum β-glucuronidase was found to be 4.1-4.2 in acetate buffer at 37°, and the assay is performed most conveniently without protein removal.

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