Purification of pure uricase enzyme of Streptomyces alboniger was carried out by Gel filtration using Sephadex G-200 column chromatography and agarose gel electrophoresis. The purification process resulted in pure protein preparation with specific activity of 2.2 units/mg protein, thus the purification process increased the concentration up to 550 fold. The molecular weight of pure uricase was 130,000 dalton as determined by polacrylamid gel electrophoresis. The purified uricase showed high activity at pH 9 and 30°C.
Also highest activity of pure enzyme was obtained after gamma irradiation at 0.5KGY, and complete inhibition of the enzyme activity occurred at 3 KGy.