Abstract

Regulation of the catalytic activity and supramolecular structure of angiotensin-converting enzyme was studied in reverse micelles of Aerosol OT in octane as biomembrane model. The kinetic experiments and the sedimentation analysis demonstrated that the enzyme can function both in monomeric and dimeric form. The degree of dimerization was strongly dependent on the concentration and structure of mono- and disaccharides added to the media, indicating the specific role of carbohydrates in forming the supramolecular structure of angiotensin-converting enzyme. The existence of carbohydrate-binding center on the enzyme molecule is proposed.

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