{"id":{"repo_id":"strathclyde","oai_identifier":"oai:strathclyde:12579s31z"},"canonical_url":"https://search.dev.ndltd.org/etd/strathclyde/oai:strathclyde:12579s31z","repository":{"repo_id":"strathclyde","name":"University of Strathclyde","base_url":"https://stax.strath.ac.uk/catalog/oai"},"display":{"title":"Investigation of preferential binding properties of monoclonal antibodies M1:1D2 and H4:4 towards the conformers of recombinant prion protein","abstract":"Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc.","abstract_html":"Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc.","abstract_has_math":false,"creators":["Nainawat, Jayant"],"institution":"University of Strathclyde","degree_name":"mres","degree_level":"masters-pg","degree_discipline":null,"degree_department":null,"school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010","date_published":"2010","updated_at":"2026-07-24T04:53:39Z","subjects":[],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier.doi","label":"DOI","values":["10.48730/z7dr-3e37"],"render_values":[{"text":"10.48730/z7dr-3e37","href":"https://doi.org/10.48730/z7dr-3e37","code":true}]},{"key":"dc:identifier","label":"Identifier","values":["T12764"],"render_values":[{"text":"T12764","href":null,"code":true}]}]},"links":{"outbound_url":"https://stax.strath.ac.uk/concern/theses/12579s31z","outbound_label":"Repository record","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:creator","label":"Author","values":["Nainawat, Jayant"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2010"]},{"key":"dc:date.issued","label":"Date","values":["2010"]},{"key":"dc:publisher.department","label":"Dc Publisher Department","values":["Strathclyde Institute of Pharmacy and Biomedical Sciences"]},{"key":"dc:publisher.institution","label":"Dc Publisher Institution","values":["University of Strathclyde"]},{"key":"dc:type.qualificationlevel","label":"Dc Type Qualificationlevel","values":["masters-pg"]},{"key":"dc:type.qualificationname","label":"Dc Type Qualificationname","values":["mres"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["T12764"]},{"key":"dc:identifier.doi","label":"DOI","values":["10.48730/z7dr-3e37"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://stax.strath.ac.uk/concern/theses/12579s31z"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["This thesis was previously held under moratorium from 10th May 2011 until 10th May 2015.","Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc."]},{"key":"dc:description.abstract","label":"Abstract","values":["Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc."]},{"key":"dc:title","label":"Title","values":["Investigation of preferential binding properties of monoclonal antibodies M1:1D2 and H4:4 towards the conformers of recombinant prion protein"]}]}],"canonical_facts":{"dc:creator":["Nainawat, Jayant"],"dc:date":["2010"],"dc:date.issued":["2010"],"dc:description":["This thesis was previously held under moratorium from 10th May 2011 until 10th May 2015.","Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc."],"dc:description.abstract":["Unlike bacteria and viruses which contain nucleic acids, prions are proteinaceous infectious agents. Prion diseases are clinically diagnosed by post-mortem histopathological examination of brain tissue and western blotting to detect proteinase K resistant prion protein. At present, no diagnostic test exists for the detection of prion diseases in live animals or humans. Use of mAbs will certainly increase sensitivity of diagnosis and it may also allow detection of PrPSc in body fluids. In this project the two mAbs M1:1D2 (IgG3) and H4:4 (IgG2a) which were raised against prion protein purified from outdated human platelets were tested for their specificity against SDS aggregated recombinant human PrP peptide. The mAbs were able to discriminate between aggregated and monomeric forms of recombinant PrP peptide and were found to be selective. These mAbs could perhaps be used in a diagnostic tool or an antibody assay against the infected or misfolded form of prion protein or PrPSc."],"dc:identifier":["T12764"],"dc:identifier.doi":["10.48730/z7dr-3e37"],"dc:identifier.uri":["https://stax.strath.ac.uk/concern/theses/12579s31z"],"dc:publisher.department":["Strathclyde Institute of Pharmacy and Biomedical Sciences"],"dc:publisher.institution":["University of Strathclyde"],"dc:title":["Investigation of preferential binding properties of monoclonal antibodies M1:1D2 and H4:4 towards the conformers of recombinant prion protein"],"dc:type.qualificationlevel":["masters-pg"],"dc:type.qualificationname":["mres"]},"updated_at":"2026-07-24T04:53:39Z"}