Affinity purification of kallikrein and elastase from hog pancrease powder.
The present report describes a method that is efficient for simultaneous isolation of kallikrein and elastase from hog pancrease powder. Both enzymes were separated by successive column chromatography on CM-cellulofine and p-aminobenzamidine-Sepharose 4B. Kallikrein was further purified by column chromatography on DEAE-Sephadex and elastase was purified by repeated gel chromatography on Sephadex G-75. The kallikrein obtained was composed of two components, which were separable by sodium dodecyl sulphate polyacrylamide gel electrophoresis, and the elastase had one component. The activity yields of kallikrein and elastase were 49 and 38%, respectively.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007610:Kallikreins / Q000302:isolation & purification*; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000302:isolation & purification*; D012967:Sodium Dodecyl Sulfate; D013552:Swine
D000596:Amino Acids; D012967:Sodium Dodecyl Sulfate; D007610:Kallikreins; D010196:Pancreatic Elastase