Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase.

@article{Hannaert2003KineticCS,
  title={Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase.},
  author={V{\'e}ronique Hannaert and Marie-Astrid Albert and Daniel J. Rigden and M Theresa da Silva Giotto and Otavio Henrique Thiemann and Richard Garratt and Joris Van Roy and Fred R. Opperdoes and Paul A. M. Michels},
  journal={European journal of biochemistry},
  year={2003},
  volume={270 15},
  pages={3205-13}
}
In this article, we report the results of an analysis of the glycolytic enzyme enolase (2-phospho-d-glycerate hydrolase) of Trypanosoma brucei. Enolase activity was detected in both bloodstream-form and procyclic insect-stage trypanosomes, although a 4.5-fold lower specific activity was found in the cultured procyclic homogenate. Subcellular localization analysis showed that the enzyme is only present in the cytosol. The T. brucei enolase was expressed in Escherichia coli and purified to… CONTINUE READING

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