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Includes abstract.
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| Format: | Thesis |
| Language: | English |
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Division of Medical Biochemistry
2014
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| _version_ | 1867613743233368064 |
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| access_status_str | Open Access |
| author | Lagardien, Zaida |
| author2 | Blackburn, Jonathan |
| author_browse | Blackburn, Jonathan Lagardien, Zaida |
| author_facet | Blackburn, Jonathan Lagardien, Zaida |
| author_sort | Lagardien, Zaida |
| collection | Thesis |
| description | Includes abstract. |
| format | Thesis |
| id | oai:open.uct.ac.za:11427/3136 |
| institution | University of Cape Town (South Africa) |
| language | eng |
| last_indexed | 2026-06-10T12:40:59.889Z |
| license_str | Not specified — see source repository |
| provenance_str_mv | Harvested via OAI-PMH from UCTD — University of Cape Town Open Access Repository |
| publishDate | 2014 |
| publishDateRange | 2014 |
| publishDateSort | 2014 |
| publisher | Division of Medical Biochemistry |
| publisherStr | Division of Medical Biochemistry |
| record_format | dspace |
| source_str | UCTD — University of Cape Town Open Access Repository |
| spelling | oai:open.uct.ac.za:11427/3136 The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen Lagardien, Zaida Blackburn, Jonathan Medical Biochemistry Includes abstract. Includes bibliographical references. Peanut agglutinin (PNA), a carbohydrate binding protein, is able to recognise and bind a number of distinct carbohydrate structures that have been implicated in a number of disease pathologies in humans. In vitro studies of PNA have previously been shown to have some specificity for the Thomson Freidenriech antigen (T-antigen), found on malignant human cells, and this specificity has made PNA an important target for protein engineering experiments aimed at improving its specificity and affinity. A number of tumour cells are characterised by altered states and patterns of glycosylation on cell surfaces and suitably engineered lectins may be able to recognise tumour specific carbohydrate structures. This study was aimed at carrying out the biophysical characterisation of a set of PNA mutants which showed apparent improvement in specificity for the T-Antigen. Previous studies have aimed to engineer this lectin in order to direct its recognition properties towards the T-antigen and away from lactose, the preliminary binding affinities of these mutants being determined using Surface Plasmon Resonance (SPR). Here a set of PNA mutants were characterised, proteins expressed and purified to determine binding activities to the T-antigen, N-Acetyl-Dlactosamine (LacNAc) and lactose through the use of Protein Micro Array technology as well as Enzyme linked immunosorbant assays (ELISA). 2014-07-28T14:55:34Z 2014-07-28T14:55:34Z 2013 Master Thesis Masters MSc http://hdl.handle.net/11427/3136 eng application/pdf Division of Medical Biochemistry Faculty of Health Sciences University of Cape Town |
| spellingShingle | Medical Biochemistry Lagardien, Zaida The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen |
| thesis_degree_str | Master's |
| title | The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen |
| title_full | The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen |
| title_fullStr | The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen |
| title_full_unstemmed | The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen |
| title_short | The characterisation of the peanut agglutinin an evolved plant lectin, with improved specificity to the Thompson Freidenriech antigen |
| title_sort | characterisation of the peanut agglutinin an evolved plant lectin with improved specificity to the thompson freidenriech antigen |
| topic | Medical Biochemistry |
| url | http://hdl.handle.net/11427/3136 |
| work_keys_str_mv | AT lagardienzaida thecharacterisationofthepeanutagglutininanevolvedplantlectinwithimprovedspecificitytothethompsonfreidenriechantigen AT lagardienzaida characterisationofthepeanutagglutininanevolvedplantlectinwithimprovedspecificitytothethompsonfreidenriechantigen |