Abstract
By preparing monoclonal antibodies (MAbs) across species it is possible to identify previously unknown molecules in a complex mixture.1 In many cases the antibody can then be used to purify the antigen it recognizes and this then opens up a wide range of structural and functional studies (Fig. 1). In particular, MAb affinity chromatography integrates with determination of protein sequence at the nucleic acid level. A limited number of peptides can be prepared from pure antigen and an oligonucleotide probe can then be synthesized from their sequence and used to detect cDNA clones for the antigen.2 The use of MAbs in affinity chromatography was first applied in studies on cell surface antigens3,4 (reviewed in Refs. 5–7) and has since been widely applied to purify molecules of all types. The steps from antigen identification with MAb to nucleotide sequence as shown in Fig. 1 have been applied to the EGF receptor,8 the IL-2 receptor,9 the MRC OX-2 antigen,10 and the leukocyte-common antigen (L-CA).11
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© 1985 Plenum Press, New York
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Johnson, P., Williams, A.F., Woollett, G.R. (1985). Purification of Membrane Glycoproteins with Monoclonal Antibody Affinity Columns. In: Springer, T.A. (eds) Hybridoma Technology in the Biosciences and Medicine. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-4964-8_9
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DOI: https://doi.org/10.1007/978-1-4684-4964-8_9
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