Allowance for antibody bivalence in the characterization of interactions by ELISA

Winzor, Donald J. (2011) Allowance for antibody bivalence in the characterization of interactions by ELISA. Journal of Molecular Recognition, 24 2: 139-148. doi:10.1002/jmr.1054


Author Winzor, Donald J.
Title Allowance for antibody bivalence in the characterization of interactions by ELISA
Journal name Journal of Molecular Recognition   Check publisher's open access policy
ISSN 0952-3499
1099-1352
Publication date 2011
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1002/jmr.1054
Open Access Status
Volume 24
Issue 2
Start page 139
End page 148
Total pages 10
Place of publication West Sussex, United Kingdom
Publisher John Wiley & Sons
Language eng
Abstract The objective of this review is to remove empiricism from the characterization of immunospecific interactions by enzyme-linked immunosorbent assay (ELISA). In place of the original presumption that the absorbance generated by the enzyme-linked assay could be regarded as a measure of free antibody concentration, the stance is taken that the parameter being monitored is the concentration of antibody complexed with immobilized antigen on the microtiter plate. After the presentation of general binding theory that takes ligand multivalence into account, that theory is adapted to incorporate the simplifying circumstances that prevail in an ELISA study. Validity of the original expressions for characterizing antigen-antibody interactions by competitive ELISA is confirmed, thereby refuting reported concerns about the need for amendment of the theoretical expressions to take into account bivalence of the antibody.
Keyword Antibody bivalence
Antigen-antibody affinity
ELISA
Solid-phase immunoassay
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collection: School of Chemistry and Molecular Biosciences
 
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