Purification and characterization of pepsins from the arctic fish capelin (Mallotus villosus).
Two pepsins from the stomach of the arctic fish capelin (Mallotus villosus) have been isolated and characterized. The purification was achieved by ammonium sulphate precipitation, ion exchange chromatography and gel filtration. Both pepsins resemble mammalian pepsins regarding pepstatin sensitivity, amino acid composition, stability and specific activity. The major capelin pepsin has optimum activity at significantly higher pH than is common for mammalian pepsins, and the optimum pH is different with different substrates. Both pepsins have relatively high activity at low temperatures. The pepsins have mol. wt of about 25,000 which is significantly lower than that of mammalian pepsins.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D005399:Fishes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D008970:Molecular Weight; D009124:Muscle Proteins / Q000378:metabolism; D010434:Pepsin A / Q000302:isolation & purification*; D010447:Peptide Hydrolases / Q000032:analysis; D012879:Skin Physiological Phenomena
D000596:Amino Acids; D009124:Muscle Proteins; D010447:Peptide Hydrolases; D010434:Pepsin A