Abstract
The proteolytic activity of elastase during solubilization of elastin is in-vestigated by measuring the release of free amino groups and the magni-tude of the average particle size. It is shown that the secondary process may be largely eliminated by elastolysis in the presence of an anionic detergent. Chemical modification of certain side-chain groups of elastin shows that the side-chain carboxy land the tyrosine hydroxyl groups are necessary for elastolysis. The former are directly concerned in ad-sorption of elastase on elastin. The amino groups are not directly con-cerned in elastolysis, but their blockage or removal gives an increase in activity probably due to the increased electronegativity of elastin. The results of chemical studies are discussed in the light of the postu-lated 2 reactions.