The identity of the elastase-associated acidic endopeptidase and chymotrypsin C from porcine pancreas.
The preparations of chymotrypsin C (EC 3.4.21.2) and an acidic endopeptidase from porcine pancreas have been repeated using published procedures. The acidic endopeptidase showed lower activity than chymotrypsin C in all comparative experiments, but it was possible to precipitate a fraction from the acidic endopeptidase preparation which contained all the protein and was identical with chymotrypsin C. It is concluded that the acidic endopeptidase is identical with chymotrypsin C but it is contaminated by an inert non-protein material to which it is firmly bound. The formation of a precipitate, at low ionic strength, from mixtures of chymotrypsin C and elastase (EC 3.4.21.11) is independent of the availability of the active site of either enzyme.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002918:Chymotrypsin / Q000302:isolation & purification / Q000378:metabolism*; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine
D000596:Amino Acids; D010450:Endopeptidases; D002918:Chymotrypsin; D010196:Pancreatic Elastase