Abstract
Several methods of preparation of soluble elastin are described and it is shown that the best material is obtained by controlled elastolysis. Coacervation is taken as best characterization of [alpha]-elastin and the most suitable conditions for the measurement of this phenomenon are investigated. The effect of detergents and elastase on this phenomenon are also studied. It is concluded that the process of coacervation of [alpha]-elastin is complex and is mainly brought about by salt-like interaction between Charged centers of the protein molecules. The kinetic studies of the reaction between [alpha]-elastin and elastase give rise to an empirical equation. It is shown that only a few reasonable assumptions and the observed facts lead to a theoretical equation which is of the same form as the empirical one. The constants of the equation have a sound physical meaning and can be obtained experimentally.