منابع مشابه
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...
متن کاملKinetics 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...
متن کاملMechanism 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...
متن کاملContribution of the intra- and intermolecular routes in autocatalytic zymogen activation: application to pepsinogen activation.
Taking as the starting point a recently suggested reaction scheme for zymogen activation involving intra- and intermolecular routes and the enzyme-zymogen complex, we carry out a complete analysis of the relative contribution of both routes in the process. This analysis suggests the definition of new dimensionless parameters allowing the elaboration, from the values of the rate constants and in...
متن کاملMechanism 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: The Journal of Biochemistry
سال: 1976
ISSN: 1756-2651,0021-924X
DOI: 10.1093/oxfordjournals.jbchem.a131099