Covalent structure of the β chain of cholera enterotoxin

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

Covalent structure of the β chain of cholera enterotoxin

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

Research output: Contribution to journal › Article › peer-review

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 language	English (US)
Pages (from-to)	7257-7264
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	252
Issue number	20
State	Published - 1977
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

Cite this

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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 Peterson, \{J. W.\}",

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, J. W.

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 - https://www.scopus.com/pages/publications/0017650211

UR - https://www.scopus.com/pages/publications/0017650211#tab=citedBy

M3 - Article

C2 - 903363

AN - SCOPUS:0017650211

SN - 0021-9258

VL - 252

SP - 7257

EP - 7264

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 20

ER -

Covalent structure of the β chain of cholera enterotoxin

Abstract

ASJC Scopus subject areas

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