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首页> 外文期刊>Journal of liquid chromatography and related technologies >Separation and purification of N-domain of bovine lung angiotensin I-converting enzyme by size exclusion chromatography
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Separation and purification of N-domain of bovine lung angiotensin I-converting enzyme by size exclusion chromatography

机译：尺寸排阻色谱法分离纯化牛肺血管紧张素I转化酶N域

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摘要

Bovine lung angiotensin-I-converting enzyme is a monomer with two active sites, in its two (N and C) homologous domains. A process is described for the preparative isolation of the ACE N-domain to either the ACE soluble monomer or ACE aggregated one. After exposure to moderate heat for 7 hours and in presence of a protease, ACE N-domain was obtained as a whole, and only fragments of the C-domain. N-domain purified was separated by Seaphacryl S-300 HR chromatography, and a recovery of 80% was obtained. Molecular mass was estimated to be 100 kDa by sodium dodecyl sulfate gel electrophoresis. After purifying and partially sepuenching this domain, we ahve investigated some catalytic properties and the inhibition by captopril.
机译：牛肺血管紧张素-I转换酶是在其两个（N和C）同源域中具有两个活性位点的单体。描述了一种将ACE N结构域制备分离为ACE可溶单体或ACE聚集单体的方法。在蛋白酶的存在下暴露于中度加热7小时后，整体获得ACE N-结构域，仅获得C-结构域的片段。通过Seaphacryl S-300 HR色谱分离纯化的N结构域，回收率达到80％。通过十二烷基硫酸钠凝胶电泳估计分子量为100kDa。纯化并部分分离该结构域后，我们研究了一些催化性质和卡托普利的抑制作用。

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