Please use this identifier to cite or link to this item: https://doi.org/10.1007/BF01980328
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dc.titleEpitope identification by polyclonal antibody from phage-displayed random peptide library
dc.contributor.authorYao, Z.-J.
dc.contributor.authorKao, M.C.C.
dc.contributor.authorChung, M.C.M.
dc.date.accessioned2014-11-27T07:42:50Z
dc.date.available2014-11-27T07:42:50Z
dc.date.issued1995
dc.identifier.citationYao, Z.-J., Kao, M.C.C., Chung, M.C.M. (1995). Epitope identification by polyclonal antibody from phage-displayed random peptide library. Journal of Protein Chemistry 14 (3) : 161-166. ScholarBank@NUS Repository. https://doi.org/10.1007/BF01980328
dc.identifier.issn02778033
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/111037
dc.description.abstractScreening of bioactive peptides from random peptide libraries using monoclonal antibodies as ligates is an effective method to define epitopes of protein antigens. However, it is thought that polyclonal antibodies might also serve as promising ligates for screening. We illustrate this approach by using recombinant human lymphotoxin (rhLT) polyclonal antibody as a model. The procedure consists in (a) affinity purification of polyclonal antibody to obtain the 'monospecific' antibody, (b) screening against a phage-displayed random peptide library using the affinity-purified antibody, (c) plating the enriched phage on agar plates, randomly picking clones, and selecting the positive ones by dot blotting, (d) DNA sequencing of the positive clones and conducting a homology search against thc protein sequence databank, and (c) confirming the epitopes by chemical peptide synthesis. By employing this procedure, we identified a dominant epitope ROHPKM, located at residues 15- 20 of the human lymphotoxin amino acid sequence. The usefulness of this general procedure is discussed.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1007/BF01980328
dc.sourceScopus
dc.subjectepitope
dc.subjecthuman lymphotoxin
dc.subjectpolyclonal antibody
dc.subjectRandom peptide library
dc.typeArticle
dc.contributor.departmentBIOPROCESSING TECHNOLOGY CENTRE
dc.description.doi10.1007/BF01980328
dc.description.sourcetitleJournal of Protein Chemistry
dc.description.volume14
dc.description.issue3
dc.description.page161-166
dc.description.codenJPCHD
dc.identifier.isiutA1995RA93900007
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