Kinetics and Mechanism of Pepsinogen Activation

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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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Mechanism of Intramolecular Activation of Pepsinogen EVIDENCE FOR AN INTERMEDIATE 6 AND THE INVOLVEMENT OF THE ACTIVE SITE OF PEPSIN IN THE INTRAMOLECULAR ACTIVATION OF PEPSINOGEN*

Intramolecular pepsinogen activation is inhibited either by pepstatin, a potent pepsin inhibitor, or by purified globin from hemoglobin, a good pepsin substrate. Also, pepsinogen at pH 2 can be bound to a pepstatin-Sepharose column and recovered as native zymogen upon elution in pH 8 buffer. Kinetic studies of the globin inhibition of pepsinogen activation show that globin binds to a pepsinogen...

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Intramolecular activation of porcine pepsinogen.

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Mechanism of intramolecular activation of pepsinogen. Evidence for an intermediate delta and the involvement of the active site of pepsin in the intramolecular activation of pepsinogen.

Intramolecular pepsinogen activation is inhibited either by pepstatin, a potent pepsin inhibitor, or by purified globin from hemoglobin, a good pepsin substrate. Also, pepsinogen at pH 2 can be bound to a pepstatin-Sepharose column and recovered as native zymogen upon elution in pH 8 buffer. Kinetic studies of the globin inhibition of pepsinogen activation show that globin binds to a pepsinogen...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1972

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)45033-3