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. 1976 Jun;30(6):881–894.

The effects of chemical modification on the antigenicity of human and rabbit immunoglobulin G.

I M Hunneyball, D R Stanworth
PMCID: PMC1445076  PMID: 68918

Abstract

In order to characterize the precise structure within human and rabbit IgG molecules against which 'general' rheumatoid factors are directed, an immunochemical comparison has been made of the effects of the selective substitution of specific amino acid side-chains on various types of antigenicity exhibited by human and rabbit IgG. The epsilon-amino groups of lysine residues have been substituted by citraconylation and carbamylation; whilst tyrosine residues have been substituted by nitration with tetranitromethane. In this manner, evidence has been obtained which indicates that the autoantigenic determinants of human IgG are structurally distinct from species-specific ones and from certain Fc-located allotypic markers (Gm(a) and Gm(x)). It is also concluded that lysine residues are probably not involved in the site of IgG reactivity with 'general' rheumatoid factors, in contrast to tyrosine residues which appear to be implicated in the activity of human but not rabbit IgG.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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