1968European Journal of BiochemistryRequires access

Thioredoxin. 6. The Amino Acid Sequence of the Protein from Escherichia coli B

Arne Holmgren

Open publisher page 276 citations

Abstract

Peptide A, the C‐terminal cyanogen bromide fragment of thioredoxin, was degraded with chymotrypsin and pepsin. Partial sequences of 12 chymotryptic and 6 peptic peptides and the N‐terminal tryptic peptide of trifluoro‐acetylated peptide A were determined. The results were used to establish the order of the previously described tryptic peptides of peptide A and lead to the complete amino acid sequence of peptide A. Previous experiments had established the amino acid sequence of peptide B, the N‐terminal cyanogen bromide fragment of thioredoxin and the present results thus give the complete amino acid sequence of thioredoxin from Escherichia coli B. The molecule contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence. The functional group of the protein occurs in position 32 to 35 and consists of a disulfide bridge formed by two half‐cystine residues separated by a glycine and a proline residue. No metals were found as part of the functional group.

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Peptide A, the C‐terminal cyanogen bromide fragment of thioredoxin, was degraded with chymotrypsin and pepsin. Partial sequences of 12 chymotryptic and 6 peptic peptides and the N‐terminal tryptic peptide of trifluoro‐acetylated peptide A were determined. The results were used to establish the order of the previously described tryptic peptides of peptide A and lead to the complete amino acid sequence of peptide A. Previous experiments had established the amino acid sequence of peptide B, the N‐terminal cyanogen bromide fragment of thioredoxin and the present results thus give the complete amino acid sequence of thioredoxin from Escherichia coli B. The molecule contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence. The functional group of the protein occurs in position 32 to 35 and consists of a disulfide bridge formed by two half‐cystine residues separated by a glycine and a proline residue. No metals were found as part of the functional group.

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Available abstract

Peptide A, the C‐terminal cyanogen bromide fragment of thioredoxin, was degraded with chymotrypsin and pepsin. Partial sequences of 12 chymotryptic and 6 peptic peptides and the N‐terminal tryptic peptide of trifluoro‐acetylated peptide A were determined. The results were used to establish the order of the previously described tryptic peptides of peptide A and lead to the complete amino acid sequence of peptide A. Previous experiments had established the amino acid sequence of peptide B, the N‐terminal cyanogen bromide fragment of thioredoxin and the present results thus give the complete amino acid sequence of thioredoxin from Escherichia coli B. The molecule contains 108 residues in a single polypeptide chain with a molecular weight of 11,657 as calculated from the sequence. The functional group of the protein occurs in position 32 to 35 and consists of a disulfide bridge formed by two half‐cystine residues separated by a glycine and a proline residue. No metals were found as part of the functional group.

Key concepts: Cyanogen bromide, Peptide sequence, Peptide, Thioredoxin, Biochemistry, Chemistry, Amino acid, Chymotrypsin

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