By N. Chiu, et. al.
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Extra info for Advances in Immunoassay Technology
N. (2002). Complementary combining site contact residue mutations of the anti-digoxin Fab 26-10 permit high affinity wild-type binding. J Biol Chem, 277(19), 16365-16370. Sidhu, S. , Weiss, G. , & Wells, J. A. (2000). High copy display of large proteins on phage for functional selections. J Mol Biol, 296(2), 487-495. Siegel, R. , & Tyner, J. (2008). Affinity maturation of tacrolimus antibody for improved immunoassay performance. Clin Chem, 54(6), 1008-1017. Skerra, A. (2007). Alternative non-antibody scaffolds for molecular recognition.
This chapter describes the designing of solid phase immunoassay using surface functionalized polyacrylonitrile fibers for the sensitive and specific determination of various antibodies. Pendent nitrile groups on polyacrylonitrile fibres were successfully reduced to generate amino groups on the surface of the fibers. The newly formed amino groups of the fibers were activated by a bi-functional spacer-glutraldehyde for the covalent linking of antibodies. Sandwich immuno-complex was developed on these PAN fibers which provided high sensitivity, specificity and reproducibility for the detection of various small analytes.
Specificity of an immunoassay does not only depend on the binding property of the antibody but also the composition of the antigen and its matrix is important. Specificity can also be influenced by reagent composition and immunoassay format. Substances that alter the measurable concentration of the analyte in the sample or alter antibody binding can potentially result in assay interference (Tate & Ward, 2004). Interference can be analyte-dependent or analyte–independent and it may increase (positive interference) or decrease (negative interference) the measured result.