Biochemical analysis of the W28F mutant of human class Pi glutathione S-transferase
No Thumbnail Available
Date
1996
Authors
Chien, Yu, Chen
Journal Title
Journal ISSN
Volume Title
Publisher
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]
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.
Keywords
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>