The protein synthesis inhibitors from wheat, barley, and rye have identical antigenic determinants.
We have purified the protein synthesis inhibitors from wheat (tritin) and investigated their antigenic relationship to inhibitors from other grains and more distantly related plants. Three forms of tritin (tritin 1, 2, and 3) indistinguishable with regards to their molecular weight and enzymatic properties were found. Antiserum against the most abundant tritin, tritin 2, cross reacted with tritin 1, tritin 3, and with the translation inhibitors from barley and rye, but not with other plant-derived translational inhibitors. The results indicate that only closely related plants contain antigenically similar protein synthesis inhibitors.
D000939:Epitopes / Q000032:analysis*; D001467:Hordeum / Q000276:immunology; D007106:Immune Sera; D005779:Immunodiffusion; D008970:Molecular Weight; D010940:Plant Proteins / Q000276:immunology* / Q000302:isolation & purification / Q000494:pharmacology; D010944:Plants / Q000276:immunology*; D014176:Protein Biosynthesis / Q000187:drug effects; D054789:Ribosome Inactivating Proteins, Type 1; D012434:Secale / Q000276:immunology; D013045:Species Specificity; D014908:Triticum / Q000276:immunology
D000939:Epitopes; D007106:Immune Sera; D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; C031676:tritin protein, Triticum aestivum