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Since the discovery more than thirty years ago that antibody
actlvlty could be localized to discrete plasma protein fractions,
the study of immunoglobulin struc ture and function has dominated
the field of immunochemistry. During this time, sources of
homogeneous immunoglobulin molecules have been discovered, the
subunit nature of the proteins has been defined, and the
three-dimensional struc tures of the antigen-recognition portion of
several antibody molecules have been elucidated. Insights into the
complicated genetic control of these proteins are being gained
rapidly through analysis of amino acid sequences of naturally
occurring and induced homogeneous immunoglobulins. Immunoglobulins
have been analyzed by protein chemists as models of complex
multimeric systems, examined by geneticists studying serum protein
polymorphisms, and employed by molecular biologists as highly
selective probes capable of distinguishing minor features of
molecular topog raphy. Clinical applications have ranged from the
now routine quantitation of immunoglobulin levels to the use of
antibodies to detect trace levels of a variety of natural products
and drug metabolites. All these applications have depended ulti
mately on a thorough understanding of the immunoglobulin and its
antigen-combin ing site. To cover the entire field of
immunoglobulin structure and function would require many volumes
this size; therefore, subjects presented in this volume represent
those which we felt contribute most to our current understanding of
this protein family. The first chapters deal with the structure and
function of the immunoglobulin molecule."
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