A novel method of isolation and some characteristic properties of human pancreatic elastases

One component of elastases of human pancreatic juice and pancreatic extract was obtained in a highly purified state by chromatography on a column of sawdust. The elastase obtained after repeated adsorption chromatography with NaCl-containing buffers was almost homogeneous by gel filtration and polyacrylamide gel electrophoresis. This elastase showed relatively high elastolytic activity, but relatively low hydrolytic activity towards succinyl trialanine p-nitroanilide, as compared with another component of pancreatic juice elastase (which was not absorbed onto sawdust). Both elastases isolated were alkaline earth metal-dependent enzymes.