Biochemical analysis of the W28F mutant of human class Pi glutathione S-transferase
| dc.contributor.author | Chien, Yu, Chen | |
| dc.date.accessioned | 2017-04-20T09:01:45Z | |
| dc.date.available | 2017-04-20T09:01:45Z | |
| dc.date.issued | 1996 | |
| dc.description | A dissertation submitted in fulfilment of the requirements for the degree of Master of Science at the University of the Witwatersrand. Johannesburg, October 1996. | en_ZA |
| dc.description.abstract | Glutathione S-transferase (GST) class Pi has two tryptophan residues which are conserved within domain one. Trp38 plays a functional role in sequestering glutathione at the active site, whereas Trp28 plays a structural role. The effects of the sterically-conservative substitution of Trp28 to Phe were investigated. When the W28F mutant was compared with the wild-type enzyme, mutation of Ttp28 to Phe was not well tolerated and resulted in a dimeric protein with impaired catalytic function and conformational stability. [Abbreviated Abstract. Open document to view full version] | en_ZA |
| dc.description.librarian | AC2017 | en_ZA |
| dc.format.extent | Online resource (136 leaves) | |
| dc.identifier.citation | Chien, Yu, Chen (1996) Biochemical analysis of the W28F mutant of human class Pi glutathione S-transferase, University of the Witwatersrand, Johannesburg, <http://hdl.handle.net/10539/22412> | |
| dc.identifier.uri | http://hdl.handle.net/10539/22412 | |
| dc.language.iso | en | en_ZA |
| dc.subject.lcsh | Glutathione transferase | |
| dc.title | Biochemical analysis of the W28F mutant of human class Pi glutathione S-transferase | en_ZA |
| dc.type | Thesis | en_ZA |
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