PH Studies on Urate Oxidase

Abstract

Two purification methods, pH precipitation and ion-exchange chromatography, were examined for suitability as steps in a purification procedure for ox-kidney urate oxidase. Neither of the methods significantly increased the specific activity of treated extracts and were thus judged as unsuitable. The action of pH on the solubility of proteins was briefly examined and some anomalies noted. These could not be explained by current theories of protein solubility. The value of dithiothreitol incubation and gel filtration was again demonstrated.