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 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...
متن کاملRational redesign of porcine pepsinogen containing an antimicrobial peptide.
A novel strategy for the controlled release and localization of bioactive peptides within digestive and immunity-related enzymes was developed. The N-terminus of porcine pepsinogen A was fused to the basic amino acid-rich region of bovine lactoferricin B termed 'tLfcB', a cationic antimicrobial/anticancer peptide. Recombinant tLfcB-porcine pepsinogen A was expressed in soluble form in Escherich...
متن کاملSynthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen.
In order to carry out studies on structure and function relationships of porcine pepsinogen using site-directed mutagenesis approaches, the cDNA of this zymogen was cloned, sequenced, expressed in Escherichia coli, and the protein refolded, and purified to homogeneity. Porcine pepsinogen cDNA, obtained from a lambda gt10 cDNA library of porcine stomach contains 1364 base pairs. It contains lead...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 1981
ISSN: 0108-7673
DOI: 10.1107/s0108767381098644