Ag-Ab Reactions and Immunology

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15 Questions

What is the definition of antibody affinity?

The force of interaction between an epitope and an antibody’s antigen binding site

What are the forces involved in forming antigen-antibody interactions?

Hydrogen bonds, hydrophobic interactions, electrostatic and van der Waals forces

Which factors can affect antibody affinity?

pH, temperature, and buffer composition

What is the difference between antibody affinity and avidity?

Affinity measures the strength of interaction between an epitope and an antibody’s antigen binding site, while avidity measures the overall strength of interaction between an antibody and all the binding sites on an antigen.

What does antibody avidity refer to?

The overall strength of interaction between an antibody and all the binding sites on an antigen

What does antibody affinity measure?

The strength of interaction between an antibody and a single antigenic determinant

What are the forces involved in forming antigen-antibody interactions?

Hydrogen bonds, hydrophobic interactions, electrostatic and van der Waals forces

Which factor does not affect antibody affinity?

The type of antigen

What is the basis for antibody specificity and cross reactivity?

Epitope recognition and binding

How is avidity of an antibody defined?

The number of antigenic determinants it can bind simultaneously

What is the equilibrium constant that describes the Ag-Ab reaction?

Affinity

What type of interactions are antigen-antibody interactions based on?

Hydrogen bonds and van der Waals forces

Which of the following factors can affect antibody affinity?

pH and buffer composition

What is the sum of the attractive and repulsive forces operating between the antigenic determinant and the combining site of the antibody called?

Affinity

What term describes antibodies being bivalent to multivalent due to having at least two antigen-binding sites?

Multivalency

Study Notes

Antibody Affinity and Avidity

  • Antibody affinity refers to the strength of binding between a single antibody-binding site and an antigenic determinant.
  • Antibody affinity measures the strength of binding between a single antibody-binding site and an antigen.
  • Antibody affinity is affected by factors such as pH, temperature, and ionic strength.
  • Hydrogen bonds, ionic bonds, van der Waals forces, and hydrophobic interactions are the forces involved in forming antigen-antibody interactions.
  • Antibody affinity differs from antibody avidity, which refers to the overall strength of binding between a multivalent antibody and an antigen.

Antibody Avidity

  • Antibody avidity describes the cumulative strength of binding between multiple antibody-binding sites and an antigen.
  • Avidity is defined as the sum of the attractive and repulsive forces operating between the antigenic determinant and the combining site of the antibody.

Antibody Specificity and Cross Reactivity

  • The basis for antibody specificity and cross-reactivity lies in the shape and chemical properties of the antigenic determinant and the antibody-binding site.

Ag-Ab Reaction

  • The equilibrium constant that describes the Ag-Ab reaction is the dissociation constant (Kd).
  • Antigen-antibody interactions are based on non-covalent interactions.

Antibody Structure

  • Antibodies can be bivalent to multivalent due to having at least two antigen-binding sites, which is described by the term valency.
  • The valency of an antibody does not affect its affinity.

Learn about antigen-antibody reactions and the principles of antibody specificity and cross-reactivity. Explore the concepts of antibody affinity and avidity, as well as commonly used tests for antigen/antibody reactions.

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