title: Catalytic properties and chemical composition of pepsins from Atlantic cod (Gadus morhua).
abstract: 1. Three pepsins were purified from the gastric mucosa of Atlantic cod (Gadus morhua). 2. The enzymes, called Pepsin I and Pepsin IIa and b, had isoelectric points 6.9, 4.0 and 4.1, respectively, and digested hemoglobin at a maximal rate at a pH of approximately 3. 3. They resembled bovine cathepsin D in being unable to digest the mammalian pepsin substrate N-acetyl-L-phenylalanyl-3,5-diiodo-L-tyrosine. 4. Specificity constants (kcat/Km) for the cod pepsins were lower than for porcine pepsin, and they expressed higher substrate affinity and physiological efficiency at pH 3.5 than at pH 2. 5. The cod pepsins are glycoproteins, and their amino acid composition resembles that of porcine cathepsin D more than that of porcine pepsin. 6. The N-terminal sequence of Atlantic cod pepsins is substantially different from that of porcine pepsin. This indicates a significant evolutionary gap between fish and mammalian pepsins.
authors.affiliation: Institute of Fisheries Technology Research, Tromsø, Norway.
authors.forename: A
authors.initials: A
authors.lastname: Gildberg
authors.forename: R L
authors.initials: RL
authors.lastname: Olsen
authors.forename: J B
authors.initials: JB
authors.lastname: Bjarnason
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002402:Cathepsin D / Q000235:genetics; D002417:Cattle; D002852:Chromatography, Ion Exchange; D005399:Fishes / Q000378:metabolism*; D005753:Gastric Mucosa / Q000201:enzymology*; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010434:Pepsin A / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013379:Substrate Specificity; D013552:Swine
chemical_list: D007527:Isoenzymes; D010434:Pepsin A; D002402:Cathepsin D