南方医科大学学报

南方医科大学学报 ›› 2015, Vol. 35 ›› Issue (02): 268-.

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硼酸盐缓冲液制备尿酸酶复合脂质体及尿酸酶的特性

周云莉，杨林，晏子俊，邓雪，张景勍   

  • 出版日期:2015-02-20 发布日期:2015-02-20

Preparation and characterization of uricase in uricase-catalase liposomes prepared using
borate buffer

  • Online:2015-02-20 Published:2015-02-20

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摘要： 目的研究硼酸-硼砂缓冲液制备的尿酸酶-过氧化氢酶脂质体（BUCLP）中尿酸酶的体外特性。方法采用逆向蒸发法制
备BUCLP，并考察其部分理化性质特性。结果BUCLP中尿酸酶最适温度保持在40 ℃，最适pH值由8.5降为8.0，而Km值也
由14.207 μmol/L降为13.623 μmol/L；尿酸酶-过氧化氢酶（UAC）与空白纳米脂质体作用后，再与FITC结合，其荧光强度高于游
离UAC与FITC结合的荧光强度，且BUCLP在280 nm处的荧光强度高于游离UAC。结论尿酸酶和过氧化氢酶联合制备成
BUCLP后尿酸酶的活性增加。

Abstract: 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 ºC, 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.