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Fatty Acid Binding Protein of Toxoplasma gondii: Isolation and Study of the Biochemical Characteristics

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Abstract

This study reports on purified and characterized fatty acid binding protein (FABP) from Toxoplasma gondi. Specifically we studied its affinity for oleic acid and calculated the different constants of association (k a), dissociation (k d) and affinity (K D), as well as the B max. This protein has a molecular mass of 14 kDa and an isoelectric point of 4.4. The equilibrium binding studies revealed a K D of 0.87 nM and a B max of 1567 pmol mg−1 of protein, a k a of 0.08 nM and a k d of 940 nM. We then studied the capacity of the protein to displace fatty acids or other hydrophobic substances and calculated the k d of each substance. The purified FABP from Toxoplasma gondii is composed of four species of protein; the 14 kDa one of which is responsible for binding the fatty acid. The mechanism involved is self-aggregation and is common to all FABP.

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Acknowledgments

This work was funded by research grant from University of Granada given to Samira Azzouz.

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Authors and Affiliations

  1. Department of Parasitology and Medical Mycology, University Claude Bernard-Lyon I, 8, avenue Rockefeller, 69373, Lyon Cedex 08, France

    Samira Azzouz, Marie Elizabeth Sarciron & Anne Françoise Petavy

  2. Department of Parasitology, Faculty of Sciences, Institute of Biotechnology, Campus Fuentenueva C.P, 18071, Granada, Spain

    Mimoun Maache & Antonio Osuna

Authors
  1. Samira Azzouz
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  2. Mimoun Maache
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  3. Antonio Osuna
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  4. Marie Elizabeth Sarciron
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  5. Anne Françoise Petavy
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Correspondence to Samira Azzouz.

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Azzouz, S., Maache, M., Osuna, A. et al. Fatty Acid Binding Protein of Toxoplasma gondii: Isolation and Study of the Biochemical Characteristics. Chroma 71, 721–725 (2010). https://doi.org/10.1365/s10337-010-1515-z

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  • DOI: https://doi.org/10.1365/s10337-010-1515-z

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