Role of Structure-Based Changes due to Somatic Mutation in Highly Homologous DNA-Binding and DNA-Hydrolyzing Autoantibodies Exemplified by A23P Substitution in the VH Domain

<table>DNA binding by BV04-01 and MRL-4 single-chain antibodies and their mutants assayed by ELISA. Vertical axis represents absorbance measured at 405 nm. Horizontal axis displays amounts of recombinant antibodies per ELISA well: 1: 5 <i>μ</i>g, 2: 1 <i>μ</i>g, 3: 0.5 <i>μ</i>g, 4: 0.1 <i>μ</i>g, 5: 0.05 <i>μ</i>g, 6: 0.01 <i>μ</i>g, 7: 0.005 <i>μ</i>g, 8 buffer without antibody. Experimental error for determined absorbance values was calculated within a series of 5-independent ELISA experiments and did not exceed 5% of medium absorbance value.</table>

Autoimmune Diseases

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Figure 2

Figure 2: Role of Structure-Based Changes due to Somatic Mutation in Highly Homologous DNA-Binding and DNA-Hydrolyzing Autoantibodies Exemplified by A23P Substitution in the VH Domain 

Figure 2 | Role of Structure-Based Changes due to Somatic Mutation in Highly Homologous DNA-Binding and DNA-Hydrolyzing Autoantibodies Exemplified by A23P Substitution in the VH Domain 