Determination of intrinsic association constant of mouse monoclonal IgM antibody to human hepatitis B surface antigen

Kim, Yung D.; Hu, R.; Mimms, Larry

doi:10.1016/0022-1759(89)90369-4

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1990

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“…Either the labelled molecules present in the supernatant or those in the sedimented immune complexes can be measured. It has been found useful to add some sucrose to the system to preserve the equilibrium during deceleration (Kim et al, 1989).…”

Section: Solution Phase Assaysmentioning

confidence: 99%

Antibody affinity measurements

Azimzadeh

Regenmortel

1990

J of Molecular Recognition

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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.

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Section: Solution Phase Assaysmentioning

confidence: 99%