Impedance spectroscopy and affinity measurement of specific antibody–antigen interaction
✍ Scribed by A. Tlili; A. Abdelghani; S. Ameur; N. Jaffrezic-Renault
- Book ID
- 103845076
- Publisher
- Elsevier Science
- Year
- 2006
- Tongue
- English
- Weight
- 124 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0928-4931
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## Various enzyme-linked immunosorbent assay or radioimmunoassay methods are currently used to quantify the antibody-antigen interaction. Only those based on indirect competition -enzyme-linked immunosorbent assay or radioimmunoassay-can provide the real thermodynamic affinity of the antibody for
In biological systems, weak-affinity interactions (association constant, K a , of less than approximately 10 4 M Ϫ 1 ) between biomolecules are common and essential to the integrity of such units. However, studies of weak biological interactions are difficult due to the scarcity of analytical method
## Abstract Bioaffinity interactions have been, and continue to be, successfully adapted from nature for use in separation and detection applications. It has been previously reported that the magnetophoretic mobility of labeled cells show a saturation type phenomenon as a function of the concentrat