Journal article
Expression of Giardia duodenalis β-Tubulin as a Soluble Protein in Escherichia coli
Protein Expression and Purification, Vol.22(1), pp.25-30
2001
Abstract
The β-tubulin gene of the parasitic protozoan Giardia duodenalis has been expressed for the first time using a novel and direct method. The protein was expressed in both soluble and insoluble forms in an Escherichia coli-based expression system. The level of expression was found to be affected by several variables including the incubation temperature, length of time for which expression was carried out, and the E. coli culture volume. The protein expression system contributed no additional amino acids to the final fusion protein and the polyhistidine fusion sequence was easily removed from the β-tubulin protein using a specific enterokinase enzyme. The expression system also provided a means of preparing a soluble protein and purifying it by a relatively straightforward affinity chromatography method to give a very high level of protein purity. This makes the protein suitable for a number of applications for characterization including β-tubulin antibody assays, α-/β-tubulin-binding regions, and β-tubulin folding intermediates.
Details
- Title
- Expression of Giardia duodenalis β-Tubulin as a Soluble Protein in Escherichia coli
- Authors/Creators
- L.M. MacDonald (Author/Creator) - Murdoch UniversityA. Armson (Author/Creator) - Murdoch UniversityR.C.A. Thompson (Author/Creator) - Murdoch UniversityJ.A. Reynoldson (Author/Creator) - Murdoch University
- Publication Details
- Protein Expression and Purification, Vol.22(1), pp.25-30
- Publisher
- Academic Press
- Identifiers
- 991005540427707891
- Copyright
- © 2001 Academic Press.
- Murdoch Affiliation
- School of Veterinary and Biomedical Sciences
- Language
- English
- Resource Type
- Journal article
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- Citation topics
- 1 Clinical & Life Sciences
- 1.163 Parasitology - General
- 1.163.1022 Anthelmintic Resistance
- Web Of Science research areas
- Biochemical Research Methods
- Biochemistry & Molecular Biology
- Biotechnology & Applied Microbiology
- ESI research areas
- Biology & Biochemistry