A general approach to standardization of the solid-phase radioimmunoassay for quantitation of class-specific antibodies
Abstract
The feasibility of using an anti-human immunoglobulin/human immunoglobulin/[125I]anti-human immunoglobulin 'sandwich' in a solid-phase radioimmunoassay to produce a standard curve which could be used to quantitate antigen-specific antibody of a particular immunoglobulin class was investigated. The amount of secondary antibody (SAb) bound was determined as a function of whether the primary antibody (PAb) was bound to its specific solid-phase antigen or by a solid-phase anti-human immunoglobulin. No significant difference between the two values was observed. Quantitation of antitetanus toxoid antibody by this method was in good agreement with quantitative precipitin tests. Comparison of SAb binding as a function of the way the PAb is bound was extended to class-specific PAb by use of murine monoclonal antibodies to meningococcal antigens. In most cases somewhat greater binding of SAb occurred when PAb was bound to antigen, but in several cases where low avidity antibody and/or poor quality antigens were used, greater SAb binding occurred when PAb was bound by anti-mouse immunoglobulin. The results indicate that this approach may be useful as a general method for standardizing the SPRIA and other solid-phase immunoassays such as t...Continue Reading
References
Citations
Safety and immunogenicity of hydrogen peroxide-inactivated pertussis toxoid in 18-month-old children
Bacterial polysaccharide immune globulin for prophylaxis of acute otitis media in high-risk children
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Antibodies produced by B cells are highly specific for antigen as a result of random gene recombination and somatic hypermutation and affinity maturation. As the main effector of the humoral immune system, antibodies can neutralize foreign cells. Find the latest research on antibody specificity here.