Abstract
A method to purify uricase from soybean root nodules is described. The separation uses a single affinity chromatography step on Arginine-Sepharose, which was constructed by coupling L-Arginine to Activated CH-Sepharose 4B. Crude extracts were loaded onto small columns of Arginine-Sepharose and a significant retardation of uricase was observed. With a re-run of the fraction containing maximal uricase activity on the same column highly purified enzyme was obtained. Analysis by SDS-polyacrylamide gel electrophoresis revealed two protein bands. Analytical isoelectric focusing showed two isoforms of uricase, one dominating with pI 9.0 and a minor with pI 7.0.
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