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Reversible Inactivation of an Intracellular Uricase From Bacillus Fastidiosus via Dissociation of Homotetramer Into Homodimers in Solutions of Low Ionic Strength

Reversible Inactivation of an Intracellular Uricase From Bacillus Fastidiosus via Dissociation of Homotetramer Into Homodimers in Solutions of Low Ionic Strength

Yunsheng Zhao, Xiaolan Yang, Xiaoyan Li, Youquan Bu, Ping Deng, Chun Zhang, Juan Feng, Yanling Xie, Sha Zhu, Huidong Yuan, Ming'an Yu, Fei Liao

Biosci Biotechnol Biochem. 2009 Sep;73(9):2141-4.

PMID: 19734651

Abstract:

An intracellular uricase from Bacillus fastidiosus with high catalytic capacity and strong resistance to xanthine was inactivated in water but could be essentially re-activated in solutions of high ionic strength. By polyacrylamide gel electrophoresis (PAGE), gradient PAGE, sodium-dodecyl-sulfate-PAGE, gel-filtration through Sephadex G200, and activity staining with peroxidase and its chromatogenic substrate, this homotetrameric uricase in water was found to dissociate into inactive homodimers that could form active homotetramers again in solutions of high ionic strength. Sensitivity to low ionic strength of solutions complicates formulation of this uricase as a drug and its elimination requires protein engineering.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP9002124	Uricase from Bacillus fastidiosus		9002-12-4	Price

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