Covalent structure of the β chain of cholera enterotoxin

A. Kurosky, D. E. Markel, J. W. Peterson

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Abstract

The complete amino acid sequence of the β chain of cholera enterotoxin was determined: NH2-THr-Pro-Gln-Asn-Ile-Thr-Asp-Leu-Cys-Ala-Glu-Tyr-His-Asn- Thr-Gln-Ile-His-Thr-Leu-Asn-Asn-Lys-Ile-Phe-Ser-Tyr-Thr-Glu-Ser-Leu-Ala-GlyLys-Arg-Glu-Met-Ala-Ile-Thr-Phe-Lys-Asn-Gly-Ala-Thr-Phe-Gln-Val-Glu-Val-Pro-Gly-Ser-Gln-His-Ile-Asp-Ser-Gln-Lys-Lys-Ala-Ile-Glu-Arg-Met-Lys-Asn-Thr- Leu-Arg-Ile-Ala-Tyr-Leu-Thr-Glu-Ala-Lys-Val-Glu-Lys-Leu-Cys-Val-Trp-Asn-Asn-Lys-Thr-Pro-His-Ala-Ile-Ala-Ala-Ile-Ser-Met-AlaMet-Ala-Asn-COOH. The sequence from automated sequence analysis of intact β-chain cyanogen bromide fragments, and a fragment generated by cleavage at a single tryptophan with 2-(2-nitrophenylsulfonyl)-3-methyl-3-bromoindolenine as well as from manual sequence analysis of tryptic peptides using 5-dimethylaminonapththalene-1-sulfonyl-monitored Edman methodology. The tryptic peptides accounted for all 103 residues established for the complete primary structure

Original languageEnglish (US)
Pages (from-to)7257-7264
Number of pages8
JournalJournal of Biological Chemistry
Volume252
Issue number20
StatePublished - Dec 1 1977

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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