Reversible inactivation of an intracellular uricase from Bacillus fastidiosus via dissociation of homotetramer into homodimers in solutions of low ionic strength.
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.
Zhao
Yunsheng
Y
Chongqing Key Laboratory of Biochemical and Molecular Pharmacology, Chongqing Medical University, Chongqing 400016, China.
Yang
Xiaolan
X
Li
Xiaoyan
X
Bu
Youquan
Y
Deng
Ping
P
Zhang
Chun
C
Feng
Juan
J
Xie
Yanling
Y
Zhu
Sha
S
Yuan
Huidong
H
Yu
Ming'an
M
Liao
Fei
F
D001407:Bacillus / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D009994:Osmolar Concentration; D012996:Solutions; D014503:Urate Oxidase / Q000037:antagonists & inhibitors* / Q000737:chemistry
D012996:Solutions; D014503:Urate Oxidase