General paperCharacterization of a chymosin-like pepsin from the dogfish Scyliorhinus canicula
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Cited by (17)
Chymosin, Pepsins and Other Aspartyl Proteinases: Structures, Functions, Catalytic Mechanism and Milk-Clotting Properties
2017, Cheese: Chemistry, Physics and Microbiology: Fourth EditionFeeding and Digestion in Elasmobranchs: Tying Diet and Physiology Together
2015, Fish PhysiologyCitation Excerpt :Gastric acid cleaves pepsinogen into pepsin, creating an active enzyme for protein digestion. Characterization of a pepsinogen in the Portuguese dogfish (Centroscymnus coelolepis) revealed a monomeric protein, ∼42 kDa in size, with similar characteristics to mammalian proteins (Nguyen et al., 1998), although activity rates of the elasmobranch protein are higher at low temperatures compared to mammalian proteins (Guerard and Le Gal, 1987). Unfortunately, the sequence of pepsinogen is not known in elasmobranchs.
The response of gastric pH and motility to fasting and feeding in free swimming blacktip reef sharks, Carcharhinus melanopterus
2007, Journal of Experimental Marine Biology and EcologyThe potential influence of gastric acid secretion during fasting on digestion time in leopard sharks (Triakis semifasciata)
2007, Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology
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