The immobilization antigen of Paramecium aurelia is a single polypeptide chain.
The immobilization antigen (i-antigen) fraction of Paramecium aurelia syngen 4 is shown to contain a protease that is activated by mercaptoethaneol. After the protease has been heat-inactivated, the molecular weight of the i-antigen (similar to 250,000 daltons) cannot be decreased by mercaptoethanol treatment. It is demonstrated that the i-antigen is a single polypeptide chain. Reasons are also given why low molecular weight subunits were previously reported by other authors.
D000941:Antigens / Q000032:analysis* / Q000302:isolation & purification; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D008623:Mercaptoethanol / Q000494:pharmacology; D008970:Molecular Weight; D010247:Paramecium / Q000254:growth & development / Q000276:immunology*; D010447:Peptide Hydrolases / Q000032:analysis; D010455:Peptides / Q000032:analysis*; D012967:Sodium Dodecyl Sulfate
D000941:Antigens; D003470:Culture Media; D010455:Peptides; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol; D010447:Peptide Hydrolases