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首页> 外文期刊>Journal of Biotechnology >Expression of the second epidermal growth factor-like domain of humanfactor VII in Escherichia coli
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Expression of the second epidermal growth factor-like domain of humanfactor VII in Escherichia coli

机译：人因子VII的第二个表皮生长因子样结构域在大肠杆菌中的表达

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摘要

The second epidermal growth factor (EGF)-like domain of human coagulation factor VII is a potent inhibitor of the FVIIa/tissue factor complex, the predominant initiator of coagulation in vivo. This domain has now for the first time been cloned and expressed in Escherichia coli as an affinity fusion protein. The fusion protein was secreted into the periplasm of E. coli and purified by affinity chromatography. The purified protein consisted of a fusion protein with the expected molecular weight, and in addition, a significant fraction of oligomers cross-linked by intermolecular disulfide bonds. Despite the presence of oligomers, the purified protein was a potent inhibitor of the extrinsic blood coagulation pathway with an IC50 value of about 20 mu M. The biological activity was retained after liberation of the EGF domain by proteolytic cleavage.
机译：人凝血因子VII的第二个表皮生长因子（EGF）样结构域是FVIIa /组织因子复合物（体内主要的凝血引发剂）的有效抑制剂。现在，该结构域首次被克隆并作为亲和融合蛋白在大肠杆菌中表达。融合蛋白被分泌到大肠杆菌的周质中并通过亲和层析纯化。纯化的蛋白质由具有预期分子量的融合蛋白质组成，此外，还有相当一部分通过分子间二硫键交联的寡聚物。尽管存在寡聚物，但纯化的蛋白还是有效的外源性凝血途径抑制剂，IC50值约为20μM。通过蛋白水解切割释放EGF结构域后，其生物学活性得以保留。

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