Conversion of pepsinogen to pepsin. Further evidence for intramolecular and pepsin-catalyzed activation.
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چکیده
منابع مشابه
Pepsinogen and Pepsin
Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is i...
متن کاملBovine 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 ...
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 کاملPepsinogen and Pepsin
Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is i...
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: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41649-9