منابع مشابه
Crystalline Pepsin Iii. Preparation of Active Crystalline Pepsin from Inactive Denatured Pepsin By
The results (1) of the experiments with crystalline pepsin isolated from crude pepsin preparations indicated that the material is a pure substance and that the proteolytic activity is a property of the protein molecule itself and is not due to the presence of a separate non-protein impurity. No indication of the presence of a more highly active nonprotein molecule was obtained in the solubility...
متن کاملStructure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s).
Using a radioimmunoassay toward the COOH-terminal region of neurotensin, an immunoreactive and biologically active neurotensin-related peptide (NRP) has been isolated from pepsin-treated fractions of bovine, canine, human, and rat plasma. Bovine NRP was identified as H-Ile-Ala-Arg-Arg-His-Pro-Tyr-Phe-Leu-OH, which is similar in structure to both neurotensin and angiotensin I. Canine and human N...
متن کاملThe substrate binding site of pepsin.
In earlier reports from this laboratory, a series of new synthetic substrates for pepsin was described.'-' These compounds are of the general type Z-His-X-YOAI\e4 where X and Y are the residues of amino acids such as L-phenylalanine, p-nitro-L-phenylalanine, L-tyrosine, L-tryptophan, and L-leucine; the enzymic action is limited to the cleavage of the X-Y bond. One of the substrate analogues pre...
متن کاملIn vitro selection and characterization of hepatitis C virus serine protease variants resistant to an active-site peptide inhibitor.
The hepatitis C virus (HCV) serine protease is necessary for viral replication and represents a valid target for developing new therapies for HCV infection. Potent and selective inhibitors of this enzyme have been identified and shown to inhibit HCV replication in tissue culture. The optimization of these inhibitors for clinical development would greatly benefit from in vitro systems for the id...
متن کاملThe pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis.
Glycine residues are known to contribute to conformational flexibility of polypeptide chains, and have been found to contribute to flexibility of some loops associated with enzymic catalysis. A comparison of porcine pepsin in zymogen, mature and inhibited forms revealed that a loop (a flap), consisting of residues 71--80, located near the active site changed its position upon substrate binding....
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1971
ISSN: 0306-3283
DOI: 10.1042/bj1230075