The trypsinogen and chymotrypsinogen contents of the pancreas during acute experimental pancreatitis of the rat.
The trypsinogen and chymotrypsinogen contents of the pancreas were examined during acute experimental pacreatitiis of the rat. The proenzymes were activated with enterokinase and the amounts of active proteases were estimated with BAPNA (N-alfa-benzoyl-DL-arginin-4-nitroanilid hydrochlorid, Fluka AG) and SUPHEPA (succinyl-L-phenylalanine-p-nitroanilide, Schwarz/Mann, Division of Becton) as the substrates. The activation of chymotrypsinogen was more rapid than the activation of trypsinogen; maximal activation occurred in 3 hours. Under similar circumstances the activation of trypsinogen required 17 hours. Both trypsinogen and chymotrypsinogen content decreased significantly during the inflammation. In 8 hours the decline of trypsinogen content was 28.4 percent and that of chymotrypsinogen content 44.9 percent from the proenzyme content of the normal resting rat pancreas. This indicates that proenzymes and/or active proteases are liberated during the course of pancreatitis. No correlation was found between the trypsinogen and the chymotrypsinogen content of the normal pancreas, but during pancreatitis the proenzyme contents correlated clearly. The correlation during inflammation possibly reflects the amount of the viable pancreatic tissue and the rate of synthesis.
D000208:Acute Disease; D000818:Animals; D002021:Buffers; D002919:Chymotrypsinogen / Q000378:metabolism*; D004765:Enteropeptidase / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D010189:Pancreatic Juice / Q000201:enzymology / Q000378:metabolism*; D010195:Pancreatitis / Q000201:enzymology / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism; D051381:Rats; D013268:Stimulation, Chemical; D013997:Time Factors; D014362:Trypsinogen / Q000378:metabolism*
D002021:Buffers; D014362:Trypsinogen; D002919:Chymotrypsinogen; D010447:Peptide Hydrolases; D004765:Enteropeptidase