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- ItemI go to seek a great perhaps: the quest to obtain an approximate understanding of steriod hormone receptor signalling(2015-04) Louw, AnnAnn Louw (née Ramsay) was born on 30 March 1957 in Vereeniging, where she grew up until the age of 13 when her parents relocated to Mexico City. She started her schooling at Drie Riviere Laerskool and Drie Riviere Hoërskool in Vereeniging, continued it at the Greengates School in Mexico City and completed Grade 13 at Forest Hill Collegiate Institute in Toronto, Canada. She returned to South Africa for her tertiary education, completing her BSc with majors in biochemistry and physiology in 1977 and her BSc Honours in 1978 at Stellenbosch University, the alma mater of both her mother, Una Ramsay (BA in 1947), and her grandfather, Eben Dönges (BA in 1918, MA in 1919). She then continued studying towards her MSc in Biochemistry while working for the Research Department of the Western Province Blood Transfusion Service (1979–1985), completing the degree cum laude in 1984. She married her husband Albé in 1980. In 1986 her son Niel was born, and she needed some time to acclimatise to parenthood. Thus she accepted part-time employment: first as part-time technical officer in the Department of Medical Biochemistry at the University of Cape Town (1987–1988) and in 1988 as part-time technical officer in the Department of Biochemistry at Stellenbosch University, where she has remained ever since. In 1990, the year her second son, Ramsay, was born, she was appointed as lecturer in the Department of Biochemistry and continued her studies under the supervision of Prof Kirsten van der Merwe and Prof Pieter Swart, receiving her PhD in 1998, the year her daughter Una was born. She was promoted to senior lecturer in 1999, to associate professor in 2009 and to full professor in 2014. Prof Louw’s research focuses on signal transduction via steroid hormone receptors, specifically the glucocorticoid receptor (GR) and the oestrogen receptor (ER), which mediate the intracellular actions of the stress hormone cortisol and the sex hormone oestrogen, respectively. Recent work on the phytooestrogenic activity of Cyclopia or honeybush tea has highlighted ER subtype-specific signalling, indicating a potential use in breast cancer prevention or treatment, while recent work on the GR is focussing on the implications of loss or gain of dimerisation.
- ItemMore than a vitamin : walks along an essential pathway(Stellenbosch : Stellenbosch University, 2014-03) Strauss, ErickErick Strauss, born on 4 November 1975 and raised in Pretoria, attended the University of Pretoria from 1994 to 1997 where he obtained his BSc (majoring in chemistry and biochemistry) and BSc(Hons) (in chemistry) degrees, both cum laude. He subsequently moved to the USA in 1998 to pursue his graduate studies at Cornell University in Ithaca, NY, where he worked on the biosynthesis of coenzyme A with Prof Tadhg Begley. He obtained a PhD in Chemistry and Chemical Biology from Cornell in 2003. He returned to South Africa in the same year to accept an offer from Stellenbosch University to establish his own research group in the Department of Chemistry and Polymer Science. In 2008 he moved to the Department of Biochemistry (also at Stellenbosch University) as associate professor, and was promoted to full professor in 2013. Since the start of his independent career he has trained 11 MSc students (one as co-supervisor) and nine PhD students (one as co-promotor); he currently leads a group of four PhD students and four postdoctoral fellows. Erick is regarded as a leading authority on the biosynthesis and enzymology of the essential metabolic cofactor coenzyme A, as well as of the design, discovery and development of antimicrobial agents that target this pathway. His publications, which have attracted a total of more than 680 citations (h-index of 12), include articles in prestigious journals such as the Proceedings of the National Academy of the USA (PNAS), the Journal of the American Chemical Society (JACS) and two articles in Nature Chemical Biology. One of these is a commentary piece chosen as one of ten winning entries (one of only two from outside the United States) submitted by young scientists active in the field in which they expounded their vision of the future ‘Grand Challenges’ in the field of Chemical Biology. Erick currently holds a B3-rating from the NRF. Erick is a recipient of the DuPont Prize for Excellence in Teaching from Cornell University (1999); the Rector’s Award for Excellence in Teaching from Stellenbosch University (2007); the President’s Award from the South African National Research Foundation (2008); the Beckman-Coulter Silver Medal from the South African Society for Biochemistry and Molecular Biology (2010); and the Raikes Medal from the South African Chemical Institute (2013). In 2012 he was elected as a founding member of the South African Young Academy of Science. Since 2009 he is also husband to Suzanne and since 2012 father to Matteo – perhaps his biggest (and ongoing!) achievements to date.
- ItemUnravelling the interconnections of cellular regulation(Stellenbosch : Stellenbosch University, 2012-10) Rohwer, Johann M.Johann Rohwer was born in Greytown on 25 May 1968 and grew up in the German settlement Hermannsburg in the KwaZulu-Natal Midlands. He received all his schooling at the Deutsche Schule Hermannsburg. After matriculating in 1985, a post-matric year (the German ‘Abitur’) at the Deutsche H¨ohere Privatschule inWindhoek followed. From 1987 to 1989 he studied for a BSc degree at Stellenbosch University, majoring in biochemistry, chemistry and mathematics. This was followed by a BScHons and an MSc in biochemistry (all cum laude), the latter under the supervision of Prof Jannie Hofmeyr, studying the regulation of serine biosynthesis in Escherichia coli. For his doctoral studies, Johann went to the Netherlands and investigated the regulation of bacterial sugar transport under the supervision of Prof HansWesterho and Dr Pieter Postma at the University of Amsterdam, graduating in April 1997. Upon his return to South Africa in 1997, Johann took up a position as Senior Lecturer in the Department of Biochemistry at Stellenbosch University and has been with the department ever since. He was promoted to Associate Professor in 2002 and to Full Professor in 2011. Under his supervision and co-supervision fourteen MSc students and seven PhD students obtained their degrees, and he has co-authored 45 peer-reviewed articles in international journals. Prof Rohwer was fortunate to spend two sabbaticals in overseas laboratories. During 2001, he visited Prof Philip Kuchel at the University of Sydney and learnt about applying the technique of NMR spectroscopy to study living cells in a non-invasive way. During 2008, he spent a year in Germany with his family as a research fellow of the Alexander von Humboldt Foundation, collaborating with Prof Mark Stitt at the Max Planck Institute of Molecular Plant Physiology on the modelling of central metabolism in plants. Johann’s research interests are computational and experimental systems biology, focusing on the analysis of the central metabolism of microbes and plants. He has received numerous awards, among others the Stellenbosch University Chancellor’s Medal (1993), the President’sAward fromthe South African National Research Foundation (2001), the Silver Medal of the South African Society of Biochemistry and Molecular Biology (2003), and the Vice Chancellor’s Award for Excellent Research from Stellenbosch University (2010). He serves on the international STRENDA Commission and on the editorial boards of BMC Systems Biology and Frontiers in Plant Systems Biology. Johann is married to Christa and they have three children–Nicola (9), Saskia (7) and Martin (19 months).
- ItemDevelopment of a synthetic affinity membrane for the purification of recombinant maltose binding proteins(Stellenbosch : Stellenbosch University, 2008-12) Asongwe, Lionel Ateh Tantoh; Swart, P.; Jacobs, E. P.; Stellenbosch University. Faculty of Science. Dept. of Biochemistry.The aim of this project was to fabricate a new affinity membrane-based system that is biospecific and biocompatible, and which could be used as an adsorption matrix for the immobilization of the recombinant protein maltose binding protein human estrogen receptor alpha ligand binding domain (MBP-hER LBD). The viability of the affinity membrane system (AMS) for the detection of estrogenic compounds (ECs) in drinking water, using affinity principles was determined. This affinity separation was based on the interaction between the analyte 17 -estradiol (E2) and the recombinant protein MBP-hER LBD. The MBP-hER LBD was immobilized on a solid matrix support. The alpha human estrogen hormone receptor (hER ) was used to test for the binding affinity of the fusion protein to a ligand, radiolabelled E2. Each component of this bioaffinity system, from the membrane matrix to the expression/purification of the bioligand, and raising of antibodies against the purified bioligand, was studied with the aim of producing a well-characterized system with the following advantages: robust in nature, cost effective and high loading capacity. Specifically, this study describes: 1. Expression of the bioligand maltose-binding protein (MBP) to be used as an affinity ligand for immobilization onto a solid membrane matrix. 2. Expression of MBP as a fusion protein to the human estrogen receptor alpha ligand binding domain (hER LBD). 3. The affinity purification of biospecific bioligands (MBP and MBP-hER LBD) using a one-step affinity purification system with amylose forming the solid phase of the affinity chromatographic column. 4. Generation of anti MBP-hER LBD antibodies to be used for the characterization of the bioligands by means of western blotting. 5. The fabrication and characterization of a flat-sheet membrane as a model affinity-matrix. 6. Developing an affinity immobilization protocol for the immobilization of the bioligand onto the affinity membrane (AM) matrix. 7. Quantitative analysis of the immobilized bioligand present on the surface of the membrane matrix using tritiated E2. The recombinant protein (MBP-hER LBD) was successfully expressed and purified to form a bio-specific ligand for its immobilization onto a cellulose acetate (CA)/amylose functionalized affinity membrane. Polyclonal antibodies were successfully raised against the purified recombinant protein. The anti-MBP-hER LBD antibodies were subsequently used as a potential ‘marker’ to confirm the immobilization of the recombinant protein onto the CA/amylose functionalized membrane. Attempts to utilize the protein-coated membrane for the selective recovery of E2 were, however, unsuccessful.