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Antibody
antigen-binding proteins produced by B cells and released in blood and lymph
Five main classes
IgA, IgD, IgE, IgG and IgM
Structure
has a quanternary structure, consisting of two heavy polypeptide chains and two light polypeptide chains arragned in a Y shape, have two antigen binding sites at the top of the arms for the same specific complementary antigen
Chains have distinct regions
constant region does not vary between antibodies or the same class and variable region that differs between antibodies
Neutralisation
antibodies bind to the surface antigens on pathogens and block their receptors to inhibit them from infecting healthy body cells
Opsonisation
bind to the surface antigens on pathogens to from antigen-antibody complexes and tag pathogen for destruction
Agglutination
bind to the surface antigens on pathogens to form antigen-antibody complexes that cause pathogens to clump together and become more visable
precipitation
antibodies bind to soluble antigens, making them insoluble
inflammation
antibodies can trigger the release of histamine causing inflammation