Abstract
The concept of antibody specificity has undergone many changes over the past 130 years, depending on the actual stand of experimental immunology. Early studies approached antibody specificity from the ligand’s side using organic chemistry to synthesize small antigenic molecules (haptens) with defined chemical structure. The structure of immunoglobulin (Ig), and its interaction with antigen were determined in the 1960s and 1970s. These studies translated the mystic concept of specificity into close structural complementarity permitting the formation of non-covalent interactions between antigen and the Ig combining site. Another aspect of specificity concerns the size of antibody repertoire required to recognize the antigenic universe. The discovery that Ig genes are assembled by random rearrangement of gene segments suggested that the potential combinatorial repertoire might be immense. But the protective biological role of antibodies places limitations on the size of the functional repertoire.
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