Premium
Protein‐chemical analysis of pertussis toxin reveals homology between the subunits S 2 and S 3 , between S 1 and the A chains of enterotoxins of Vibrio cholerae and Escherichia coli and identifies S 2 as the haptoglobin‐binding subunit
Author(s) -
Capiau Carine,
Petre Jean,
Van Damme Jozef,
Puype Magda,
Vandekerckhove Joël
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80839-0
Subject(s) - pertussis toxin , toxin , homology (biology) , enterotoxin , chemistry , protein subunit , g protein , biochemistry , gene , escherichia coli , receptor
The purified toxin of Bordetella pertussis was dissociated in 5 M urea in the presence of immobilized haptoglobin. The toxin was dissociated in free S 1 , free S 5 and the free complexes S 2 ‐S 4 and S 3 ‐S 4 , with S 2 ‐S 4 as the only haptoglobin‐binding moiety, identifying S 2 as the haptoglobin‐binding protein. Partial NH 2 ‐terminal amino acid sequences were obtained from the dissimilar toxin subunits, after separation by SDS‐polyacrylamide gel electrophoresis followed by electroblotting onto polybrene‐coated glass‐fiber sheets. The sequences reveal extensive homology of the N‐terminal portions of the constitutive subunits S 2 and S 3 and between S 1 and the enterotoxin A chains of Vibrio cholerae and Escherichia coli .