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. 1982 Aug;46(4):751–760.

Theoretical and ultracentrifugal analysis of immune complex formation between monoclonal antibodies and human IgG.

J Steensgaard, C Jacobsen, J Lowe, N R Ling, R Jefferis
PMCID: PMC1555474  PMID: 6179855

Abstract

Immune complex formation of four different mouse monoclonal antibodies against human IgG has been studied using analytical zonal centrifugation. A theoretical model has been used to depict thermodynamic ideal immune complex formation of monoclonal antibodies. It was found that the four monoclonal antibodies differed very much with respect to immune complex formation with human IgG. One of the monoclonal antibodies formed immune complexes in agreement with the theoretical model. Another was strongly related thereto. A third monoclonal antibody formed only a single complex and might exhibit a positive co-operativity between its two sites. A fourth formed as excess of a possibly cyclic complex. Thus monoclonal antibodies differ substantially with respect to physical properties adding a new aspect to the problems of antibody heterogeneity. It is moreover found that analytical zonal centrifugation can be used to estimate the number of antigenic determinants and antibody-binding sites thereby assuring whether or not a particular IgG monoclonal antibody has two binding sites.

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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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