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Pancreatic proteolytic enzymes from carp cyprinus carpio 2. kinetic properties and inhibition studies of trypsin chymotrypsin and elastase



Pancreatic proteolytic enzymes from carp cyprinus carpio 2. kinetic properties and inhibition studies of trypsin chymotrypsin and elastase



Comparative Biochemistry and Physiology B 69(3): 647-753



Kinetic parameters for hydrolysis of specific synthetic substrates by carp (C. carpio) trypsin, chymotrypsin and elastase were determined and compared to the respective mammalian enzymes. The kinetic properties of carp and mammalian trypsin and elastase were quite similar. The differences between the respective chymotrypsins were bigger probably due to minor differences in the vicinity of the catalytic site. The pH dependency of the enzymatic activities was determined in the pH range 3-11. These most likely result from the dissociation of histidine-57 and the N-terminal amino group. Carp trypsin and chymotrypsin were irreversibly inhibited by amino acid and peptide chloromethylketones, thus further indicating the involvement of histidine-57 in the active site. A partial mapping of chymotrypsin with peptide chloromethylketones suggested the existence of an extended binding site. Inhibition of carp trypsin, chrymotrypsin and elastase by 8 naturally occurring high-molecular proteinase inhibitors resulted in inhibition curves resembling the respective bovine or porcine enzymes. Carp trypsin possibly interacts also with the chymotrypsin site of several inhibitors.

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