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.
D002413:Cations, Divalent / Q000494:pharmacology; D002845:Chromatography / Q000379:methods; D006801:Humans; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D002413:Cations, Divalent; D010196:Pancreatic Elastase