Biochemistry detection of acetylcholinesterase activity in Trypanosoma evansi and possible functional correlations

[Display omitted] ► Acetylcholinesterase (AChE) is an important enzyme that hydrolyzes of acetylcholine. ► AChE is broadly distributed in many species, including parasites. ► In the present study we could demonstrate, by biochemistry technical, that the Trypanosoma evansi expresses the enzyme AChE....

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Veröffentlicht in:Experimental parasitology 2012-12, Vol.132 (4), p.546-549
Hauptverfasser: Wolkmer, Patrícia, da Silva, Cássia B., Paim, Francine C., Da Silva, Aleksandro S., Tavares, Kaio C.S., Lazzarotto, Cícera R., Palma, Heloisa E., Thomé, Gustavo R., Miletti, Luiz C., Schetinger, Maria Rosa C., Lopes, Sonia T.A., Mazzanti, Cinthia M.
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Sprache:eng
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Zusammenfassung:[Display omitted] ► Acetylcholinesterase (AChE) is an important enzyme that hydrolyzes of acetylcholine. ► AChE is broadly distributed in many species, including parasites. ► In the present study we could demonstrate, by biochemistry technical, that the Trypanosoma evansi expresses the enzyme AChE. Several chemical and immunohistochemical techniques can be used for the detection of acetylcholinesterase (AChE) activity. In this experiment we aimed to detect AChE activity in Trypanosoma evansi. For this, the parasites were isolated from the blood of experimentally infected rats using a DEA-cellulose column. Enzymatic activity was determined in trypomastigote forms at 0, 0.2, 0.4, 0.8 and 1.2mg/mL of protein concentrations by a standard biochemical protocol. At all concentrations tested, the study showed that T. evansi expresses the enzyme AChE and its activity was proportional to the concentration of protein, ranging between 0.64 and 2.70μmol of AcSCh/h. Therefore, we concluded that it is possible to biochemically detect AChE in T. evansi, an enzyme that may be associated with vital functions of the parasite and also can be related to chemotherapy treatments, as further discussed in this article.
ISSN:0014-4894
1090-2449
DOI:10.1016/j.exppara.2012.08.015