Intramolecular Activation of Porcine Pepsinogen
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چکیده
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...
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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 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...
متن کاملThe amino-terminal sequence of porcine pepsinogen.
Amino acid sequence studies were performed on (a) peptides obtained from tryptic hydrolysates of succinyl pepsinogen and (b) those isolated from a peptide mixture formed when pepsinogen is activated to pepsin. These peptides taken together with tryptic peptides obtained from reduced carboxymethylated pepsinogen establish the complete sequence of 41 residues at the NH&erminal end of the single p...
متن کاملExpression of soluble cloned porcine pepsinogen A in Escherichia coli.
A system for the production of soluble porcine pepsinogen A (EC 3.4.23.1) was developed by fusing the pepsinogen and thioredoxin genes and then expressing the fused product (Trx-PG) in Escherichia coli. The expressed fusion protein was purified using a combination of ion-exchange and hydrophobic chromatography. Trypsin digestion of the fusion protein yielded pepsinogen which was one residue lon...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62458-5