Electrophoretic study of the caseinolytic activity of a pepsin from the dogfish Scyliorhinus canicula.
Electrophoretic patterns of casein and casein subfractions were studied following proteolysis by dogfish pepsin II or calf chymosin. Both enzymes hydrolyze the kappa casein subfraction with the production of kappa paracasein peptide. alpha S1 and beta subfractions hydrolysis is stronger with dogfish enzyme than with chymosin. It is concluded that, despite a broader specificity, the activity spectrum of dogfish enzyme is, in many respects, similar to that of calf chymosin.
Guerard
F
F
Laboratoire de Biologie Marine, Collège de France, Concarneau.
Le Gal
Y
Y
D000818:Animals; D002364:Caseins / Q000378:metabolism*; D002417:Cattle; D012085:Chymosin / Q000378:metabolism*; D004284:Dogfish / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007700:Kinetics; D010434:Pepsin A / Q000378:metabolism*; D012754:Sharks / Q000378:metabolism*
D002364:Caseins; D010434:Pepsin A; D012085:Chymosin