The Variation And Adaptive Expression Of Antibodies

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The Variation and Adaptive Expression of Antibodies

Author: George P. Smith
language: en
Publisher: Harvard University Press
Release Date: 1973
During the past ten years, several theories have been proposed on the origin of the diversity of antibodies. George P. Smith presents a critical study of these theories in this detailed treatment of immunological problems from the point of view of molecular genetics. Mr. Smith uses a new and simplifying approach to this long-standing controversy. By a comprehensive computerized analysis of antibody amino acid sequences (particularly the myeloma proteins), the author traces their evolution and matches his results against the expectations of the various theories of diversity. He discusses at length the other types of evidence as well. Mr. Smith also deals with the clonal specialization of cells to produce a single antibody, and the relationship of this specialization to the somatic joining of antibody half-genes, which is one of the immune system's most important peculiarities. Introductory material is provided to make this work understandable to molecular geneticists not versed in immunology and to immunologists not versed in molecular genetics. This is a timely book offering a succinct and coherent summary of the various lines of evidence in a confused and controversial field.
Immunoglobulins

Author: Gary Litman
language: en
Publisher: Springer Science & Business Media
Release Date: 2012-12-06
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.
The Antibody Enigma

Author: Thomas Kindt
language: en
Publisher: Springer Science & Business Media
Release Date: 2012-12-06
The Antibody Enigma is a somewhat personal view of the antibody diversity question from two investigators who have spent the past 18 years trying to penetrate the enigma. It is not and was not meant to be an all-embracing comprehensively referenced review of the subject of antibody diversity. Because of the subjective viewpoint, there are un doubtedly omissions of data that others consider to be seminal, and if we have offended anyone by omitting their own contribution we sin cerelyapologize. We have lived with "The Enigma" on and off for the past two years. It has been both hard work and good fun but, above all, it has been a learning experience. There were several difficult decisions to make in putting together the final text, but perhaps the most difficult was de ciding upon a stopping point. The field of antibody diversity is presently enjoying an unparalleled expansion of information, and because of this it was very tempting to await further developments in hopes of tying up as many loose ends as possible. This was decided against for several reasons; the major factor was that the project was growing burdensome for both of us. From a more objective point of view this appears to be a reasonable time to stop our exposition.