Antigen
In immunology, antigens (Ag) are structures (aka substances) specifically bound by antibodies (Ab) or a cell surface version of Ab ~ B cell antigen receptor (BCR). The term antigen originally described a structural molecule that binds specifically to an antibody only in the form of native antigen. It was expanded later to refer to any molecule or a linear molecular fragment after processing the native antigen that can be recognized by T-cell receptor (TCR). BCR and TCR are both highly variable antigen receptors diversified by somatic V(D)J recombination. Both T cells and B cells are cellular components of adaptive immunity. The Ag abbreviation stands for an antibody generator.
Snake antivenom
Compositions of the antivenom can be classified as whole IgG, or fragments of IgG. Whole antibody products consist of the entire antibody molecule, often immunoglobulin G (IgG), whereas antibody fragments are derived by digesting the whole IgG into Fab (monomeric binding) or F(ab')2 (dimeric binding). The fragment antigen binding, or Fab, is the selective antigen binding region. An antibody, such as IgG, can be digested by papain to produce three fragments: two Fab fragments and one Fc fragment. An antibody can also be digested by pepsin to produce two fragments: a F(ab') fragment and a pFc' fragment.
The fragment antigen-binding (Fab fragment) is a region on an antibody that binds to antigens, such as venoms. The molecular size of Fab is approximately 50kDa, making it smaller than F(ab') which is approximately 110kDa. These size differences greatly affect the tissue distribution and rates of elimination.