Back to Search
Start Over
Antibody affinity measurements
- Source :
- Journal of molecular recognition : JMR. 3(3)
- Publication Year :
- 1990
-
Abstract
- The use of antibodies in immunoaffinity separations represents one of the most specific methods for purifying substances of biological interest. Since the binding affinity of antibody greatly influences its behavior in such separations, it is often important to know the value of the antibody affinity expressed as an equilibrium constant K. The present review discusses the equations used in the quantitative analysis of antigen/antibody interactions and describes currently used experimental methods for measuring K values. Advantages and shortcomings of the solution phase and solid phase approaches used for measuring antibody affinity are discussed.
- Subjects :
- Immunoassay
Chromatography
medicine.diagnostic_test
biology
Chemistry
Antibody Affinity
Antibody affinity
Antigen-Antibody Reactions
Solutions
Kinetics
Antigen
Affinity chromatography
Structural Biology
medicine
biology.protein
Binding Sites, Antibody
Binding site
Antibody
Molecular Biology
Quantitative analysis (chemistry)
Equilibrium constant
Subjects
Details
- ISSN :
- 09523499
- Volume :
- 3
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Journal of molecular recognition : JMR
- Accession number :
- edsair.doi.dedup.....8ddcdf8cb1fccd2933c5014b5d5a4f16