- Title
- Analysis of the interaction between recombinant human Beta2 integrin I-domains and CD23
- Creator
- Sprong, Kaitlin
- Subject
- Immune response -- Regulation
- Subject
- Immunoglobulins
- Subject
- CD23 antigen
- Date Issued
- 2014
- Date
- 2014
- Type
- Thesis
- Type
- Masters
- Type
- MSc
- Identifier
- vital:10362
- Identifier
- http://hdl.handle.net/10948/d1021078
- Description
- In order to further elucidate the interaction between CD23 and β2 integrins (CD11b/CD18) the following objectives were established: Expression and purification of CD11b I-domain as a GST-fusion protein using Escherichia coli; Cloning, synthesis and expression of CD18 I-Like domain.CD11b I-domain has previously been expressed as a GST-fusion protein (Daniels, 2010) and consequently led to comparable expression of CD18 I-like domain as a GST-fusion protein; Preparation of two site-directed mutants of CD18 I-Like domain in order to study the function of the serine residue involved in the S116P mutation. The serine was mutated to proline, as in LAD patients, as well as alanine, a non-polar alternative, in order to contrast and compare binding characteristics. Expression, refolding and purification of sCD23, and a double mutatedsCD23 (RKΔAA) from E. coli; This was performed according to the method described by Daniels et al. (2005); Investigation of the CD23-CD11b I-like domain interaction through surface plasmon resonance spectroscopy.
- Format
- xi, 124 leaves
- Format
- Publisher
- Nelson Mandela Metropolitan University
- Publisher
- Faculty of Science
- Language
- English
- Rights
- Nelson Mandela Metropolitan University
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NMMU School of BioMolecular and Chemical Sciences
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