Solid phase synthesis of two cholera toxin B subunit antigens.
The 30-50 and 50-75 sequences of the cholera toxin beta 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.
D000818:Animals; D000942:Antigens, Bacterial / Q000032:analysis*; D002199:Capillary Permeability / Q000187:drug effects; D002772:Cholera Toxin / Q000138:chemical synthesis* / Q000276:immunology / Q000494:pharmacology; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D051379:Mice; D008810:Mice, Inbred C57BL
D000942:Antigens, Bacterial; D002772:Cholera Toxin