Immunoglobulin Y in the chicken is functionally equivalent to Immunoglobulin G (IgG). It is composed of two light and two heavy chains. the difference is that the heavy chains of IgY are larger than those in IgG. The light chains in IgY are smaller than the light chains in IgG. The molar mass of IgY is about 167,000 amu. Its steric flexibility is somewhat less than that of IgG.
IgY is partially comparable to Immunoglobulin E (IgE), as well as to IgG, in functionality. In contrast to IgG, however, IgY does not bind to Protein A or G, or to cellular Fc receptors. In addition, IgY does not activate the complement system.
IgY cross-reacts much less with mammalian protein than does IgG. In addition, conserved mammalian proteins often are more immunogenic in birds than in mammals.
The only immunoglobulin found in chicken eggs is IgY, from amongst all the other immunoglobulins that are generated during the immune response. There is no contamination from Immunoglobulin A (IgA) or Immunoglobulin M (IgM).
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