Characterization of a chymosin-like pepsin from the dogfish Scyliorhinus canicula.
1. Pepsin II extracted from the gastric mucosa of Scyliorhinus canicula has been characterized and compared to calf chymosin. 2. The kcat and Km of the dogfish enzyme for the synthetic hexapeptide Leu-Ser-Phe(NO2)-Nle-Ala-Leu-OMe have been determined. The kcat/Km ratio is close to that of calf chymosin. Its milk-clotting efficiency is however 21-fold lower than that of calf chymosin. 3. The proteolytic activity against haemoglobin is optimal at pH 2.5. It clots the milk up to pH 6.8. 4. The dogfish pepsin II shows relatively better activity at low temperatures than calf chymosin.
D000818:Animals; D012085:Chymosin / Q000378:metabolism; D004284:Dogfish / Q000378:metabolism*; D005753:Gastric Mucosa / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010434:Pepsin A / Q000378:metabolism*; D012754:Sharks / Q000378:metabolism*; D013379:Substrate Specificity
D010434:Pepsin A; D012085:Chymosin