Covalent structure of the β chain of cholera enterotoxin

A. Kurosky, D. E. Markel, Johnny Peterson

Research output: Contribution to journalArticle

36 Citations (Scopus)

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 - 1977

Fingerprint

Cyanogen Bromide
Protein Sequence Analysis
Tryptophan
Sequence Analysis
Amino Acid Sequence
Peptides
Amino Acids
Vibrio cholerae stN protein

ASJC Scopus subject areas

  • Biochemistry

Cite this

Covalent structure of the β chain of cholera enterotoxin. / Kurosky, A.; Markel, D. E.; Peterson, Johnny.

In: Journal of Biological Chemistry, Vol. 252, No. 20, 1977, p. 7257-7264.

Research output: Contribution to journalArticle

Kurosky, A. ; Markel, D. E. ; Peterson, Johnny. / Covalent structure of the β chain of cholera enterotoxin. In: Journal of Biological Chemistry. 1977 ; Vol. 252, No. 20. pp. 7257-7264.
@article{4c9b26fa48ad48abb82e54e5774fcb81,
title = "Covalent structure of the β chain of cholera enterotoxin",
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",
author = "A. Kurosky and Markel, {D. E.} and Johnny Peterson",
year = "1977",
language = "English (US)",
volume = "252",
pages = "7257--7264",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "20",

}

TY - JOUR

T1 - Covalent structure of the β chain of cholera enterotoxin

AU - Kurosky, A.

AU - Markel, D. E.

AU - Peterson, Johnny

PY - 1977

Y1 - 1977

N2 - 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

AB - 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

UR - http://www.scopus.com/inward/record.url?scp=0017650211&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0017650211&partnerID=8YFLogxK

M3 - Article

VL - 252

SP - 7257

EP - 7264

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 20

ER -