| Popis: |
The behaviors of proteases were examined in the pancreatic juice pooled into a closed duodenal loop and it was confirmed that the activation of proteases occurred quickly after the operation. Three kinds of pancreatic proteases, trypsin, kallikrein and elastase were purified from the pancreatic juice by succesive isoelectric focusing, Soya-bean trypsin inhibitor-Sepharose 4B affinity and Sephadex G-100 column chromatographies. Apparent molecular weights of the purified trypsin, kallikrein and elastase were 26,000, 31,000 and 25,000, respectively. Their isoelectric points were 5.0, 5.0 and 8.0, and their specific activities were 490 TAMe units, 45 TAMe units and 0.47 elastinolytic units/mg protein, respectively. All of these proteases induced a reflux pancreatitis in mongrel dogs and the reflux pancreatitis by the infusion of trypsin was the severest. |
