The Activation of Bovine Pepsinogen

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Bovine Pepsinogen and Pepsin

As the first step in the investigation of the structure and action of little known gastric zymogens and enzymes, pepsinogen has been isolated from the mucosa of the fourth stomach (abomasum) of the’ cow. The pepsinogen was purified by ammonium sulfate fractionation, batch absorption on diethylaminoethyl (DEAE) cellulose, recycling gel filtration on Sephadex G-100, and finally chromatography on ...

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The activation of bovine pepsinogen. Sequence of the peptides released, identification of a pepsin inhibitor.

Bovine pepsinogen is converted into pepsin by removal of 45 amino acid residues from the NH, terminus of the single polypeptide chain. The complete sequence of the activation peptides has been deduced from two overlapping sets of peptides, one set obtained by autoactivation of the zymogen at pH 2 and the second set from a tryptic digest of maleylated pepsinogen. A peptide derived from the 17 re...

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Bovine pepsinogen and pepsin. I. Isolation, purification, and some properties of the pepsinogen.

As the first step in the investigation of the structure and action of little known gastric zymogens and enzymes, pepsinogen has been isolated from the mucosa of the fourth stomach (abomasum) of the’ cow. The pepsinogen was purified by ammonium sulfate fractionation, batch absorption on diethylaminoethyl (DEAE) cellulose, recycling gel filtration on Sephadex G-100, and finally chromatography on ...

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Intramolecular activation of porcine pepsinogen.

Conversion of pepsinogen to pepsin at acid pH involves an intramolecular reaction in which the unproteolyzed zymogen cleaves itself. This conclusion is based upon experiments in which pepsinogen, at low concentrations, was activated in the presence of substrate, hemoglobin. Under these conditions, the activation of pepsinogen is independent of pepsinogen concentration, and addition of pepsin do...

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Kinetics and mechanism of pepsinogen activation.

The spontaneous and pepsin-catalyzed activation of pepsinogen has been observed and analyzed kinetically. At appropriate protein concentrations (1 mg per ml or less), a kinetically first order reaction was observed in the pH range 1 to 3, implying an intramolecular activation mechanism. Substantiation of the first order reaction came from a linear plot of log pepsinogen concentration versus tim...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1974

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)42445-9