The structural features responsible for the immunogenicity of
certain parts of native protein molecules have been of interest to
immunochemists and protein chemists for over three decades.
Following the early work of Land steiner in 1942, which showed that
peptide fragments from silk fibroin exhibited an inhibitory
activity toward the reaction of the protein with its antibodies,
fragments from many other protein systems have been isolated and
studied. However, no concerted effort was (or could be) devoted to
the elucidation of the complete antigenic structure of a protein.
In order for these endeavors to be successful and meaningful,
knowledge of both the amino acid sequence and the detailed
three-dimensional structure of the protein is necessary. Such
information was not available for a protein until early in the
1960s. This and the fact that protein chemistry was not in fact
sufficiently developed early in the 1960s to enable the successful
completion of the entire antigenic structure of a protein were
major contributing factors for the slow progress in this field.
Determination of the antigenic structures of proteins therefore
posed a chemical challenge of enormous proportions. For these
reasons, many investigators diverted their attention to study of
the immunochemistry of homo- or mixed amino acid polymers in the
hope that the information derived from these systems might prove
useful in the understanding of the immunochemistry of proteins."
General
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