The isolation and characterization of pepsinogens from the proventriculus of the ostrich Struthio camelus.
Three pepsinogens were isolated and purified from the proventriculus of the ostrich Struthio camelus, by a combination of chromatography steps on DEAE-cellulose, Sephadex G-100 and Hydroxylapatite. The purified pepsinogens manifested peptic activity towards haemoglobin as substrate after activation, but resembled chicken pepsinogens in that they appeared to lose their potential peptic activities during storage. All three pepsinogens contained glycine as N-terminal amino acid, but differed in their overall amino acid compositions. The pH and temperature optima of the activated pepsinogens were determined, as well as their molecular weights.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001717:Birds / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D010435:Pepsinogens / Q000302:isolation & purification* / Q000378:metabolism; D011531:Proventriculus / Q000201:enzymology*; D013816:Thermodynamics
D000596:Amino Acids; D007527:Isoenzymes; D010435:Pepsinogens