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Updated: Apr 16, 2026
Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
Published on: April 5, 2018
[Preparation and characterization of uricase in uricase-catalase liposomes prepared using borate buffer]
Yunli Zhou1, Lin Yang, Zijun Yan
1Medicine Engineering Research Center, Key Laboratory of Biochemical & Molecular Pharmacology, Chongqing Medical University, Chongqing 400016, China.E-mail: zhouyunli716@163.com.
Objective:
To characterize the property of uricase loaded in uricase-catalase liposomes (BUCLPs) prepared using borate buffer.
Methods:
BUCLPs were prepared using reverse-phase evaporation, and the physicochemical properties of uricase in the prepared BUCLPs were examined.
Results:
The optimal temperature of BUCLP and URI was 40 degrees celsius, their optimal pH values were 8.0 and 8.5, and their Michaelis-Menten constants were 14.207 µmol/L and 13.623 µmol/L, respectively. Fluorescence intensity of nanoliposome-loaded uricase-catalase that bound to FITC was higher than that of uricase-catalase binding directly with FITC; the fluorescence intensity of BUCLP was higher than that of free uricase-catalase at 280 nm.
Conclusion:
Uricase activity is enhanced after loading in uricase and catalase liposomes.
