Abstract
Genome analysis of Entamoeba histolytica predicts the presence of acetyl-CoA carboxylase. Using Western blot, histochemistry, and confocal microscopy, we demonstrated the presence of a biotin-containing protein in the cytoplasm of E. histolytica, with a molecular weight of 136 kDa and biotin–carboxylase activity. This protein probably corresponds to a transcarboxylase that catalyzes the rate-limiting reaction leading to fatty acid elongation.
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Acknowledgments
We thank Bruce Allan Larsen for reviewing the use of English in this manuscript and Teresita Cruz Hernández for technical support. This work was supported in part by grants from SEPI-IPN. A. Salas-Casas, A. Jarillo-Luna, L. Mendoza-Alcantar, E. Abarca-Rojano, and R. Campos-Rodríguez are fellows of COFAA and DEPI-IPN.
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Barbosa-Cabrera, E., Salas-Casas, A., Rojas-Hernández, S. et al. Purification and cellular localization of the Entamoeba histolytica transcarboxylase. Parasitol Res 111, 1401–1405 (2012). https://doi.org/10.1007/s00436-012-2898-6
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DOI: https://doi.org/10.1007/s00436-012-2898-6