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structure
globular glycoproteins with quaternary structure
made of 2 heavy + 2 light polypeptide chains joined by disulfide bridges
constant region: same for all antibodies in 1 class, determines destruction method
variable region: different per antibody, forms antigen binding site
-specific to epitope on antigens
-specificity due to different amino acid sequences
hinge region: in heavy polypeptide chain, gives flexibility to bind to antigens at diff. angles
antigen=antibody complexes
antibody collides with cell with complementary foreign non-self antigens → binds to form antigen-antibody complex
Y-shaped antibodies have 2 antigen binding sites → can bind to over 1 cell at same time
-groups of pathogens can clump together in agglutination
binding of antibodies to antigen neutralises pathogen/ acts as marker to attract phagocytes for phagocytosis
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