RESUMO
Regulation of the catalytic activity and the supramolecular structure of the angiotensin-converting enzyme isolated from bovine lungs has been studied in a system of reversed micelles of aerosol OT (AOT) in octane. The curve for the dependence of the enzyme catalytic activity on the degree of the surfactant hydration (micellar size) has two maxima at the hydration degrees of [H2O]/[AOT] 27 and 31. Data from velocity sedimentation suggest that depending on the hydration degree, the angiotensin-converting enzyme occurs in the system of reversed micelles in both monomeric and dimeric forms, the latter being catalytically active. In contrast with aqueous media, in the reversed micelle system the angiotensin-converting enzyme does not require chloride anions for its catalytic activity. In the system of reversed micelles of AOT in octane the holoenzyme is stable, while the apoenzyme rapidly and irreversibly loses its activity. Under these conditions the apoenzyme shows an ability to incorporate the Zn2+ ions into the enzyme active center; however, only in the presence of a substrate or an inhibitor.
