Andujar-Sánchez M, Cámara-Artigas A, Jara-Pérez V
Dpto. Química Física, Bioquímica y Qui;mica Inorgánica, Universidad de Almería, Carretera Sacramento s/n, 04120, Almería, Spain.
J Chromatogr B Analyt Technol Biomed Life Sci. 2003 Jan 5;783(1):247-52. doi: 10.1016/s1570-0232(02)00663-3.
Angiotensin I converting enzyme (ACE) plays a major role in blood pressure regulation, catalyzing the conversion of angiotensin I to the vasoconstrictor angiotensin II. In this report we describe a two-step affinity chromatography method for preparative purification of ACE from pig lung using Concanavalin-A Sepharose 4B and affinity chromatography on Lisinopril Sepharose 6B. The same purification scheme was used to obtain Cobalt-ACE, where zinc ion located at the active site is replaced by cobalt. Cobalt-ACE visible spectrum shows a characteristic broad peak from 500 to 600 nm. The shape and maximum absorptivity of this peak changes in presence of ACE inhibitors that bind at the catalytic site.
血管紧张素I转换酶（ACE）在血压调节中起主要作用，催化血管紧张素I转化为血管收缩剂血管紧张素II。在本报告中，我们描述了一种两步亲和色谱法，用于从猪肺中制备纯化ACE，该方法使用伴刀豆球蛋白A琼脂糖4B和赖诺普利琼脂糖6B进行亲和色谱。采用相同的纯化方案获得钴-ACE，其中位于活性位点的锌离子被钴取代。钴-ACE可见光谱在500至600nm处显示出特征性的宽峰。在结合于催化位点的ACE抑制剂存在下，该峰的形状和最大吸光度会发生变化。
