Comparison of the structure of the immunoglobulins from horse serum.
A study of the chemical structure of the horse immunoglobulins IgG and IgA(T) has shown that the amino acid contents of the peptide chains are very similar. These globulins differ most markedly in the products of papain digestion. IgG gives 3.5s products, whereas IgA(T) gives a 5s fraction and smaller components. This difference appears to be associated with the presence of an additional easily reducible disulphide bond in the Fd fragment of the heavy chain. There is two to three times as much carbohydrate in IgA(T) as in IgG. In both, this is in the heavy chain and in IgA(T) more than half is covalently bound to the Fd fragment. The differences in antigenic specificity between horse IgG and IgA(T) appear to be due to structural differences in the Fc fragment.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000941:Antigens; D003013:Clostridium; D004167:Diphtheria Toxin; D006736:Horses; D007106:Immune Sera; D007120:Immunochemistry; D007122:Immunoelectrophoresis; D010206:Papain / Q000494:pharmacology*; D010455:Peptides / Q000032:analysis; D013745:Tetanus Toxoid
D000596:Amino Acids; D000941:Antigens; D004167:Diphtheria Toxin; D007106:Immune Sera; D010455:Peptides; D013745:Tetanus Toxoid; D010206:Papain