Studies on Yeast Uricase

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Abstract
A method for obtaining a highly purified preparation of yeast uricase was developed. The procedure included extraction of uricase from the uric ase-induced yeast cells, fractionation with ammonium sulfate and chromatography on a DEAE-cellulose column. The purified yeast uricase was shown to be ultracentrifugally homogeneous. The enzyme acted best at pH 8.5 and was stable in a range from pH 7.0 to 11.0 and at temperatures lower than 40°G. The Michaelis constant for urate was calculated to be 5.88 × 10−6 m at pH 8.5, borate buffer. Activity and stability of the enzyme, however, were found to be significantly affected by the kind of buffer used. The enzyme was sensitive to heavy metal ions such as mercuric and cupric ions, but the sensitivity was influenced by the kind of buffer used.

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