Selective inhibition of elastolytic and proteolytic properties of elastase

The elastolytic and proteolytic (fibrin, casein, and hemoglobin) properties of elastase, purified by CM-cellulose chromatography and electrophoretically homogeneous at pH's 9.0 and 4.5, could be selectively inhibited. Soybean trypsin inhibitor and kallikrein inactivator substantially suppressed proteolytic activity of the enzyme, but were without influence on its elastolytic properties. Conversely, elastolysis was substantially suppressed by high molar salt concentration, whereas proteolysis was not influenced thereby. These results suggest either the presence of several enzymes with similar chromatographic and electrophorctic properties, or else that elastase has more than one active center, one directed against as yet unspecified regions or linkages of elastin, the other having broad and more classical proteolytic properties.