ABSTRACT
Elastase from human pancreas was purified by ion-exchange and affinity chromatography with an 85% yield and to approximately 95% homogenicity as judged by discontinuous slab-gel electrophoresis. The human enzyme differed in chemical and enzymatic properties in comparison to porcine pancreatic elastase. Human elastase antiserum exhibited no cross-reactivity with porcine elastase, but precipitated the human enzyme. The human elastase possessed 25% of the enzymatic activity of porcine elastase in solubilizing alkaline-extracted bovine elastin, but solubilized human aortic elastin at a much higher rate. The results initially suggested a substrate specificity by human elastase for human elastin, but additional data indicated that the method of purification of elastins significantly affected the rates of solubilization by both human and porcine pancreatic elastase.
