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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts.

An amino acid sequence analysis of the N-terminal immunoglobulin heavy and light chain variable regions (VH and VL) from 16 hybridoma proteins which bind phosphorylcholine as well as the complete sequence analysis of 9 of these VH regions is presented. There seem to be more VH regions participating in the phosphorylcholine response than can be encoded directly by germ-line VH gene segments. Moreover, the V regions from IgG antibodies are considerably more variable than those from their IgM counterparts. These observations raise the possibility that a somatic mechanism for V region diversification produces greater diversity in IgG than in IgM antibodies.[1]

References

  1. IgG antibodies to phosphorylcholine exhibit more diversity than their IgM counterparts. Gearhart, P.J., Johnson, N.D., Douglas, R., Hood, L. Nature (1981) [Pubmed]
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