Abstract
Glutathione S-transferase activity has been shown to be associated with the microsomal fraction of Taenia solium. Electron microscopy and subcellular enzyme markers indicate the purity of the microsomal fraction that contains the glutathione S-transferase activity. T. solium microsomes were solubilized under conditions used to solubilize integral microsomal proteins. This procedure proved necessary to obtain enzymatic activity. To characterize this parasite enzyme activity, several substrates and inhibitors were used. The optimum activity for microsomal glutathione S-transferase was found to be pH 6.6, with a specific enzyme activity of 0.9, 0.1, 0.067, 0.03, and 0.05 μmol min−1 mg−1 with the substrates 1-chloro-2,4-dinitrobenzene (CDNB), 1,2-dichloro-4-nitrobenzene, 4-hydroxynonenal, 2,4-hexadienal, and trans-2-nonenal, respectively. No activity of glutathione peroxidase was observed. T. solium microsomes had an app K m (GSH) = 0.161 μM, app K m (CDNB) = 14.5 μM, and app V max of 0.15 and 27.9 μmol min−1 mg−1 for GSH and CDNB, respectively. T. solium microsomes were inhibited by several glutathione S-transferase enzyme inhibitors, and it was possible to establish a simple inhibition system as well as corresponding K i ’s for each inhibitor. These results indicate that the T. solium microsomal glutathione S-transferase is different from the parasite cytoplasmic enzymes that catalyze similar reactions.
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Acknowledgments
The authors wish to thank Dr. Gerardo Medina for valuable English corrections. We thank Dra. Irene P. del Arenal, who kindly assisted us during the succinate dehydrogenase measurement. The present study was funded by grant from Universidad Nacional Autónoma de México, DGAPA (PAPIIT-IN201906-3). All the experiments complied with the current laws of the Universidad Nacional Autónoma de México.
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Nava, G., Robert, L. & Plancarte, A. Characterization of Taenia solium cysticerci microsomal glutathione S-transferase activity. Parasitol Res 101, 1373–1381 (2007). https://doi.org/10.1007/s00436-007-0655-z
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DOI: https://doi.org/10.1007/s00436-007-0655-z