Solid phase synthesis of two cholera toxin B subunit antigens
- 1 April 1985
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 25 (4) , 421-424
- https://doi.org/10.1111/j.1399-3011.1985.tb02195.x
Abstract
The 30–50 and 50–75 sequences of the cholera toxin β chain including the amino-acids that are thought to be involved in toxin-receptor binding have been synthesized using the solid phase method. They were then purified by gel permeation and ion exchange chromatography. Both these free peptides induced serum antibodies recognising the native toxin after oral or intraperitoneal administration. Only the antibodies raised against the 50–75 peptide, however, were able to neutralize toxin activity.Keywords
This publication has 16 references indexed in Scilit:
- Priming for and induction of anti-poliovirus neutralizing antibodies by synthetic peptidesNature, 1983
- Role of membrane gangliosides in the binding and action of bacterial toxinsThe Journal of Membrane Biology, 1982
- Prediction of protein antigenic determinants from amino acid sequences.Proceedings of the National Academy of Sciences, 1981
- Active antitoxic immunization by a diphtheria toxin synthetic oligopeptideNature, 1981
- Involvement of arginine residues in the binding site of cholera toxin subunit BBiochemical and Biophysical Research Communications, 1979
- Synthesis of a nonadecapeptide corresponding to residues 37-55 of ovine prolactin. Detection and isolation of the sulfonium form of methionine-containing peptidesJournal of the American Chemical Society, 1976
- The arrangement of subunits in chlorea toxinBiochemistry, 1976
- The Preparation of Merrifield‐Resins Through Total Esterification With Cesium SaltsHelvetica Chimica Acta, 1973
- The monitoring of reactions in solid-phase peptide synthesis with picric acidAnalytica Chimica Acta, 1972
- Deactivation of Cholera Toxin by GangliosideThe Journal of Infectious Diseases, 1971