重组大肠杆菌菌株产生一种展示生物聚酯颗粒的ZZ结构域，适用于免疫球蛋白G的纯化。
Recombinant Escherichia coli strain produces a ZZ domain displaying biopolyester granules suitable for immunoglobulin G purification.
作者信息
Brockelbank Jane A, Peters Verena, Rehm Bernd H A
机构信息
Institute of Molecular Biosciences, Massey University, Private Bag 11222, Palmerston North, New Zealand.
出版信息
Appl Environ Microbiol. 2006 Nov;72(11):7394-7. doi: 10.1128/AEM.01014-06. Epub 2006 Aug 25.
Abstract
The immunoglobulin G (IgG) binding ZZ domain of protein A from Staphylococcus aureus was fused to the N terminus of the polyhydroxyalkanoate (PHA) synthase from Cupriavidus necator. The fusion protein was confirmed by matrix-assisted laser desorption ionization-time-of-flight mass spectrometry and mediated formation of ZZ domain-displaying PHA granules in recombinant Escherichia coli. The IgG binding capacity of isolated granules was assessed using enzyme-linked immunosorbent assay and could be enhanced by the overproduction of the ZZ-PHA synthase. ZZ-PHA granules enabled efficient purification of IgG from human serum.
摘要
来自金黄色葡萄球菌的蛋白A的免疫球蛋白G（IgG）结合ZZ结构域与来自食酸戴尔福特菌的聚羟基脂肪酸酯（PHA）合酶的N端融合。通过基质辅助激光解吸电离飞行时间质谱法确认了融合蛋白，并介导了重组大肠杆菌中展示ZZ结构域的PHA颗粒的形成。使用酶联免疫吸附测定法评估了分离颗粒的IgG结合能力，并且可以通过过量表达ZZ-PHA合酶来增强。ZZ-PHA颗粒能够从人血清中高效纯化IgG。
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