What are the effects of antigen-antibody interactions?
Antigen-antibody interactions can result in a variety of consequences, including precipitation of soluble antigens, agglutination of particulate antigens, neutralization of toxins and viruses, and activation of complement.
When is an antigen-antibody precipitate is formed?
Antigen- antibody precipitate is formed in the zone where the concentration of the two matching pair reaches an optimal known as the zone of equivalence. Those regions of precipitation can be used for determination of concentration or titer of both antigen and antibody. Two techniques use the principle of immunodiffusion. 1.
How to make be-antibody in 10 P L buffer?
1. Add 700 P l TAE buffer to the BE -Antigen 1 vial. Soak the antigen for 5 minutes with periodically vortexing to dissolve the antigen completely. 2. Label 6 tubes with Antigen and aliquot in 10 P l antigen solution. Supply each group with one vial of Antigen. 3. Add 65 P l TAE buffer to each vial containing the BE -Antibody 1.
How is avidity used to describe antigen-antibody interaction?
Another term used to describe antigen-antibody interaction is AVIDITY. Avidity is the strength of multiple interactions between antigen and antibody with multiple binding sites. All antibodies have at least two antigen binding sites represented as their (Fab) 2.
Where does diffusion occur in an antigen-antibody interaction?
Due to antigen being in excess, diffusion occurs until a stable ring of antigen- antibody precipitate forms. The line of precipitation is the site where the greatest number of complexes are formed, at the zone of equivalence. The diame ter of the endpoint precipitation ring corresponds to the amount of antibody in the sample.
How many binding sites are there in an antibody?
Avidity is the strength of multiple interactions between antigen and antibody with multiple binding sites. All antibodies have at least two antigen binding sites represented as their (Fab) 2.