Chemical modification of carboxyl groups in porcine pepsin

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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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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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Amino-acid sequence of porcine pepsin.

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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Carboxyl-terminal sequence of human gastricsin and pepsin.

The tryptic peptides from human pepsin and gastricsin were purified and their sequences were determined. The sequence of 27 residues at the COOH-terminal end of human pepsin was found to be: -Ile-Leu-Gly-Asp-Val-Phe-Ile-ArgGln-Phe-Tyr-Thr-Val-Phe-Asp-Arg-Ala-Asn-Asn-GlnVal-Gly-Leu-Ala-Pro-Val-Ala. The sequence of 19 residues at the COOH-terminal end of human gastricsin was found to be: -Gln-Phe...

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Chemical modification of corn fiber with ion-exchanging groups

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ژورنال

عنوان ژورنال: Journal of Agricultural and Food Chemistry

سال: 1980

ISSN: 0021-8561,1520-5118

DOI: 10.1021/jf60230a017