Specificity and evolutionary divergence of the antigenic structure of the polypeptide chain elongation factors.
Antisera have been prepared against two electrophoretically homogeneous "polypeptide chain elongation factors," T and G, from Escherichia coli. Inactivation and precipitation tests showed that these two fractions were antigenically distinct with no cross-reaction. The immune inactivation curve of G factor from E. coli was distinguishable from that of G factor from Pseudomonas fluorescens. Mammalian factors were not inhibited by antibody directed against the E. coli T and G factors. By Ouchterlony diffusion tests, the antisera also detected significant antigenic variability among different bacterial species. It is concluded that the factors have undergone considerable evolutionary divergence in their antigenic structure.
D000941:Antigens / Q000032:analysis*; D001419:Bacteria / Q000276:immunology*; D005075:Biological Evolution; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000276:immunology; D007106:Immune Sera; D005779:Immunodiffusion; D010455:Peptides / Q000032:analysis*; D010649:Phenylalanine / Q000096:biosynthesis; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis; D011549:Pseudomonas / Q000276:immunology
D000941:Antigens; D007106:Immune Sera; D010455:Peptides; D010649:Phenylalanine; D010744:Phosphoric Monoester Hydrolases