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Titlebook: Epitope Mapping Protocols; Glenn E. Morris Book 1996 Humana Press 1996

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書目名稱Epitope Mapping Protocols
編輯Glenn E. Morris
視頻videohttp://file.papertrans.cn/314/313383/313383.mp4
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: Epitope Mapping Protocols;  Glenn E. Morris Book 1996 Humana Press 1996
描述Interest in epitope mapping, or finding out where antibodies bind to their antigens, is by no means restricted to immunologists, but is shared by biolo- gists from a wide range of disciplines in which antibodies are used as molecu- lar reagents. The epitope mapper may be interested in studying protein-protein interactions, in developing an immunoassay, in producing protective peptide vaccines, in investigating the pathogenesis of autoimmune diseases, or in defining protein topology in intact cells or organelles, to mention only a few of the possibilities. The aim of Epitope Mapping Protocols is to provide both a useful range of alternative practical methods for the experienced mapper and a fairly com- prehensive introduction for someone embarking on antibody production and mapping for the first time. Contributors were encouraged to illustrate their protocols with results from their own research and most of them elected to do so. After an introductory chapter, the protocols are arranged in three groups: The first group of twelve methods uses (or can use) whole, native antigens and may therefore be suitable for conformational epitopes; the second group of five uses peptides or peptid
出版日期Book 1996
版次1
doihttps://doi.org/10.1385/0896033759
isbn_softcover978-0-89603-375-7
isbn_ebook978-1-59259-552-5Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightHumana Press 1996
The information of publication is updating

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A Simple Solid-Phase Competition Assay with Labeled Antigen, the antigen is immobilized, and a radiolabeled antibody and competing unlabeled antibodies are mixed in solution (.) (.,.). Although this method facilitates separation of free from bound antibody, it possesses the problem of labeling all antibodies to be tested. Since the number of MAbs to be scree
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Identifying Residues in Antigenic Determinants by Chemical Modification, proteolytic fragmentation, it played a major role in the pioneering efforts of Atassi and others to assign antigenic determinants on the surfaces of lysozyme and myoglobin (.,.). The principle of the method is that alteration of the structure of a key residue in an epitope by a chemical modificatio
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Epitope Mapping by Differential Chemical Modification of Antigens, in three-dimensional space. In the case of antibodies to native proteins, most or perhaps all epitopes are discontinuous (.). Because of the large size of a typical contact epitope in an antigen-antibody crystal, it is unlikely for an antibody to bind exclusively to a contiguous stretch of the poly
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Proteolytic Fragmentation for Epitope Mapping,dely used to provide antibodies with a defined specificity. One characteristic feature of this technology is that impure antigens can be used to produce monospecific antibodies that can be utilized to study the functional domains of protein molecules. In this chapter, the use of limited vs complete
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