Nondenaturing solubilization of β2 microglobulin from inclusion bodies by L-arginine
Nondenaturing solubilization of β2 microglobulin from inclusion bodies by L-arginine
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DOI：
10.1016/j.bbrc.2004.12.156
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发表时间：
2005-03-04
影响因子：
3.1
通讯作者：
Kumagai, I
中科院分区：
文献类型：
--
作者：
Umetsu, M;Tsumoto, K;Kumagai, I
β 2微球蛋白（β 2 m）在大肠杆菌中的表达导致包涵体的形成。衰减全反射傅里叶变换红外分析表明，在包涵体中的β 2 m的天然二级结构。用L-精氨酸溶液非变性增溶包涵体中的天然样β 2 m，可有效回收β 2 m，且几乎不发生聚集。在较高的温度下，从包涵体中获得更大的β 2 m增溶。低温增溶产生的β 2 m的荧光特性相同的天然β 2 m，但其二级结构略有规范。在中等温度下溶解得到具有明显天然结构的β 2 m。本文提出了一种将L-精氨酸与中温相结合的高效非变性增溶方法。(C)2005年爱思唯尔公司All rights reserved.
Expression of beta2 microglobulin (beta2m) in Escherichia coli resulted in formation of inclusion bodies. Attenuated total reflectance Fourier transform infrared analysis suggested a native-like secondary structure of beta2m in the inclusion bodies. Nondenaturing solubilization of the native-like beta2m from inclusion bodies was achieved Using L-arginine solution, which enables all efficient recovery of beta2m with little aggregation. Greater beta2m solubilization from inclusion bodies was obtained at higher temperatures. Low-temperature solubilization yielded beta2m with fluorescence properties identical to those of native beta2m, but its secondary structure was slightly normative. Solubilization at moderate temperature gave beta2m with an apparently native structure. We propose ail efficient nondenaturing solubilization method combining L-arginine and moderate temperature. (C) 2005 Elsevier Inc. All rights reserved.