ANGIOTENSIN-CONVERTING ENZYME IN THE SYST EM OF REVERSED MICELLES OF DOCUSATE SODIUM IN OCTANE - INTERACTION WITH THE MATRIX

Regulation of catalytic activity and intramolecular structure of the b ovine lung angiotensin-converting enzyme was studied using reversed mi celles in a sodium docusate-water-octane system, which model the enzym e's environment in vivo. The catalytic parameters of monomeric and dim eric forms of the enzyme in the reversed micellar system were evaluate d. The catalytic activity of die angiotensin-converting enzyme extract ed from bovine lung with Triton X-100 did not depend on the detergent concentration at a constant level of hydration. An artificially hydrop hobized form of the angiotensin-converting enzyme was obtained by modi fying the enzyme with stearic acid chloride. The modification leads to the dependence of the catalytic activity on the surfactant concentrat ion, which provides evidence that the enzyme interacts with the micell ar matrix. The modified enzyme showed a significant increase in cataly tic activity in the reversed micellar system.