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. 1973 Oct;15(2):145–152.

The binding affinities of rheumatoid factors interacting with the Cγ3 homology region of human IgG

M W Steward, M W Turner, J B Natvig, P I Gaarder
PMCID: PMC1553889  PMID: 4202647

Abstract

The binding affinities of rheumatoid factors interacting with Gm(a), Gm(x), `non a' and `γ4 non a' antigens have been measured by an equilibrium molecular sieving technique using rheumatoid sera of known specificity and pFc' fragments (≡Cγ3 homology region) from IgG molecules of defined subclass and allotype. All the rheumatoid factors studied showed specific binding with the fragments possessing the homologous antigen. The binding affinities of these rheumatoid factors were low, between 104 and 105 litres/mole. In contrast, no binding occurred between rheumatoid factors and fragments lacking the appropriate antigenic determinant.

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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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