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Purification of angiotensin I converting enzyme from pig lung using concanavalin-A sepharose chromatography

2002; Elsevier BV; Volume: 783; Issue: 1 Linguagem: Inglês

10.1016/s1570-0232(02)00663-3

1873-376X

Montserrat Andújar‐Sánchez, A. Cámara-Artigas, Vicente Jara‐Pérez,

Biochemical effects in animals

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.