Abstract
Uricase (urate: oxygen oxidoreductase; EC 1.7.3.3) from the rust Puccinia recondita was purified to electrophoretic homogeneity. Preparations with a specific activity of 8.4 U/mg were used for characterization of the enzyme, which showed a strong similarity to other plant and fungal urate oxidases. The enzyme had a pH optimum of 9.0, a K m of 35 μM for urate, and it was inhibited only by oxonate and xanthine. A molecular mass of 152 kDa was estimated for the native protein. SDS-PAGE analysis revealed a striking difference to most urate oxidases, since two different-sized subunits were detected. These results suggest that P. recondita uricase is a tetramer with two types of subunits.
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Received: 21 February 2001 / Accepted: 30 July 2001
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Aguilar, M., Montalbini, P. & Pineda, M. Urate Oxidase from the Rust Puccinia recondita Is a Heterotetramer with Two Different-Sized Monomers. Curr Microbiol 44, 257–261 (2002). https://doi.org/10.1007/s00284-001-0101-x
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DOI: https://doi.org/10.1007/s00284-001-0101-x