Trypsin from Greenland cod, Gadus ogac. Isolation and comparative properties.
Trypsin(ogen) was isolated from the pyloric ceca of Greenland cod. Greenland cod trypsin catalyzed hydrolysis of N alpha-benzoyl-DL-arginine p-nitroanilide, tosyl arginine methyl ester and protein and was inhibited by the serine protease inhibitor PMSF and other well-known trypsin inhibitors. Greenland cod trypsin was more stable at alkaline pH than at acid pH; and was inactivated by relatively low thermal treatment. Like other trypsins, the enzyme was rich in potential acidic amino acid residues but poor in basic amino acid residues and had a molecular weight of 23,500; but it had less potential disulfide pairs, less alpha-helix and a lower H phi ave than other trypsins previously characterized. Reactions catalyzed by Greenland cod trypsin were not very responsive to temperature change, such that specific activity was relatively high at low reaction temperature.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004789:Enzyme Activation; D005399:Fishes; D006116:Greenland; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D011708:Pylorus / Q000201:enzymology*; D013379:Substrate Specificity; D014357:Trypsin / Q000302:isolation & purification* / Q000378:metabolism; D014362:Trypsinogen / Q000378:metabolism
D000596:Amino Acids; D014362:Trypsinogen; D014357:Trypsin