Refolding and recovery of recombinant human matrix metalloproteinase 7 (Matrilysin) from inclusion bodies expressed by Escherichia coli
Refolding and recovery of recombinant human matrix metalloproteinase 7 (Matrilysin) from inclusion bodies expressed by Escherichia coli
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DOI：
10.1093/oxfordjournals.jbchem.a022533
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发表时间：
1999-11-01
影响因子：
2.7
通讯作者：
Inouye, K
中科院分区：
文献类型：
--
作者：
Oneda, H;Inouye, K
重组人基质金属蛋白酶7 （matrilysin或MMP-7）在大肠杆菌中以不溶性包涵体的形式过表达。6 M胍基HCI溶解后，用100倍稀释重新折叠重组蛋白。通过基质溶素活性的恢复来监测再折叠。添加1.0 M精氨酸或0.1% Brij-35均能显著促进再折叠。再折叠与pH和温度有关，温度越低(
The recombinant prepro-form of human matrix metalloproteinase 7 (matrilysin or MMP-7) was overexpressed in Escherichia coli as insoluble inclusion bodies. The recombinant protein was refolded by 100-fold dilution after solubilization with 6 M guanidine HCI. The refolding was monitored by the recovery of matrilysin activity. The addition of either 1.0 M arginine or 0.1% Brij-35 promoted remarkably the refolding. The refolding was dependent on pH and temperature, with lower temperature (