Engineering of Porcine Pepsin

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The carboxyl-terminal sequence of porcine pepsin.

The sequence of 27 residues at the carboxyl end of the single polypeptide chain of porcine pepsin has been found to be: -Ile-Leu-Gly-Asp-Val-Phe-Ile-Arg-Gln-Tyr-Tyr-ThrVal-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ala-ProVal-Ala. The peptides from which this sequence has been derived were isolated from tryptic and chymotryptic digests of pepsin and its reduced aminoethylated and trifluoracetylate...

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As the culmination of several years of experiments, we propose a complete amino-acid sequence for porcine pepsin, an enzyme containing 327 amino-acid residues in a single polypeptide chain. In the sequence determination, the enzyme was treated with cyanogen bromide. Five resulting fragments were purified. The amino-acid sequence of four of the fragments accounted for 290 residues. Because the s...

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Fluorescence studies on the active sites of porcine pepsin and Rhizopus-pepsin.

Fluorescence studies on the interaction, with porcine pepsin, of oligopeptides bearing a mansyl (Mns, 6-(N-methylanilino)-2-naphthalenesulfonyl) or dansyl (Dns, 5-dimethylaminonaphthalene-1-sulfonyl) group at the NH2 or COOH terminus have provided further evidence showing that the probe group is drawn into the extended active site largely as a consequence of the specific binding of the peptide ...

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Chemical modification of carboxyl groups in porcine pepsin.

Carboxyl groups i n porcine pepsin were chemically modified "by the carbodiimide reaction using waterrsoluble l-ethyl-3-(3-dimethylaminopropyl) carbodiimide and amino acid esters as nucleophiles. The modification resulted in profound changes in the a c t i v i t i e s , specificity and.some physicochemical properties of the enzyme. These include* (1) significant decrease in milk clotting activi...

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Primary structure of porcine pepsin. III. Amino acid sequence of a cyanogen bromide fragment, CB2A, and the complete structure of porcine pepsin.

The complete amino acid sequence of porcine pepsin (EC 3.4.4.1) was constructed from the sequence of five cyanogen bromide fragments. The sequence of one of these fragments, CB2A, is reported here. The sequences of 4 other fragments are known from previous work. Porcine pepsin contains 327 residues with three structural variants. The active center aspartyl residue, which reacts with 1,2-epoxy-3...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1997

ISSN: 0021-9258

DOI: 10.1074/jbc.272.30.18855