Improved method for pro-urokinase refolding with inclusion body from recombinant Escherichia coli

被引:1
作者
Kubo, M [1 ]
Nishi, A [1 ]
机构
[1] TOSOH CORP,SCI INSTRUMENT DEV DEP,AYASE,KANAGAWA 252,JAPAN
来源
JOURNAL OF FERMENTATION AND BIOENGINEERING | 1995年 / 80卷 / 06期
关键词
protein folding; pro-urokinase; inclusion body; recombinant protein;
D O I
10.1016/0922-338X(96)87745-2
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
We developed an efficient inclusion body pro-urokinase refolding method from recombinant Escherichia coli. The protein was efficiently refolded when a heat treatment was applied to a protein denaturing solution containing guanidine hydrochloride. The total enzyme activity and the specific activity in response to the 50 degrees C heat treatment compared to normal method (25 degrees C) were enhanced about 10 and 25%, respectively. Moreover, enhanced protein refolding was also observed in the case of a reduced protein concentration in the protein refolding solution. The result indicates that correct protein folding is closely related to the protein concentration in the refolding solution.
引用
收藏
页码:622 / 624
页数:3
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