title: Interrelationships between toxins: studies on the cross-reactivity between bacterial or animal toxins and monoclonal antibodies to two jellyfish venoms.
abstract: Affinity chromatography on columns of immobilized anti-Chrysaora and anti-Physalia monoclonal antibodies can be an effective purification tool for animal and bacterial toxins. Furthermore, the fact that specific fractions of a given species obtained from immunochromatography columns prepared with either monoclonal antibody possessed identical protein bands, were quantitatively similar in in vitro cardiotoxicity and bound like amounts of antibody, as indicated by the enzyme-linked immunosorbent assay, suggested that antigenic targets of the two monoclonal antibodies are cross-reactive and/or are located on the same molecule. Additional enzyme-linked immunosorbent assays were conducted using non-coelenterate toxins. The significant binding of brown recluse spider venom and purified cholera toxin to both our monoclonal antibodies indicated that these toxic substances shared a common or cross-reacting antigenic site(s) with some coelenterate venoms.
authors.forename: C E
authors.initials: CE
authors.lastname: Olson
authors.forename: M G
authors.initials: MG
authors.lastname: Heard
authors.forename: G J
authors.initials: GJ
authors.lastname: Calton
authors.forename: J W
authors.initials: JW
authors.lastname: Burnett
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000032:analysis*; D000918:Antibody Specificity; D001427:Bacterial Toxins / Q000276:immunology* / Q000633:toxicity; D002642:Chick Embryo; D003064:Cnidarian Venoms / Q000276:immunology* / Q000633:toxicity; D003429:Cross Reactions; D004591:Electrophoresis, Polyacrylamide Gel; D004797:Enzyme-Linked Immunosorbent Assay; D013111:Spider Venoms / Q000276:immunology / Q000633:toxicity; D014118:Toxins, Biological / Q000276:immunology*
chemical_list: D000911:Antibodies, Monoclonal; D001427:Bacterial Toxins; D003064:Cnidarian Venoms; D013111:Spider Venoms; D014118:Toxins, Biological