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Enzymes comparison based on proteomics on organisms

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Ascorbate Peroxidase in Trypanosoma cruzi Structures, Functions, and its
Contribution to Cause Chagas Disease.

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Ascorbate Peroxidase in Trypanosoma cruzi Structures, Functions, and its
Contribution to Cause Chagas Disease.
Introduction
The protozoan Trypanosoma cruzi is the single-cell parasite known to cause Chagas
disease, a tropical infection. It is an emerging public health hazard has in the U.S. for causing
many cases of premature deaths. Chagas disease is only treatable by two drugs, nifurtimox, and
benznidazole. However, these drugs are unsatisfactory due to the toxic side effects and efficacy
they possess. Benznidazole cures the disease when it is in the acute stage though it cannot cure
the disease in the chronic phase (Agmon et al., 2018). Nifurtimox and benznidazole use can lead
to cross-resistance. Besides, 30 % of adult individuals experience chronic Chagas infection with
mega digestive syndromes and cardiomyopathy symptoms (Agmon et al., 2018).
By sequence analysis, Trypanosoma cruzi ascorbate peroxidase falls under class 1 heme
peroxidase, a member of a hybrid type A. for the establishment of the infection, parasite
antioxidant systems are crucial (Arlian, Morgan and Rider, 2016). Catalase and selenium are
enzymes capable of metabolizing hydrogen peroxide, are not found in Trypanosoma cruzi.
Trypanosoma cruzi antioxidant defense system systems are different from their host.
Biochemical and morphological changes occur during the Trypanosoma cruzi life cycle (Bogacz
and Krauth-Siegel, 2018).
In the endoplasmic reticulum of Trypanosomatids, there is one ascorbate peroxidase
isoform. However, through studies, there is still an unknown advantage of ascorbate peroxidase
to the infection potential and virulence of Trypanosoma cruzi (Bogacz and Krauth-Siegel, 2018).
Besides, proteomic studies suggest an increase in expression in the infectious forms referred to

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1 Ascorbate Peroxidase in Trypanosoma cruzi Structures, Functions, and its Contribution to Cause Chagas Disease. 2 Ascorbate Peroxidase in Trypanosoma cruzi Structures, Functions, and its Contribution to Cause Chagas Disease. Introduction The protozoan Trypanosoma cruzi is the single-cell parasite known to cause Chagas disease, a tropical infection. It is an emerging public health hazard has in the U.S. for causing many cases of premature deaths. Chagas disease is only treatable by two drugs, nifurtimox, and benznidazole. However, these drugs are unsatisfactory due to the toxic side effects and efficacy they possess. Benznidazole cures the disease when it is in the acute stage though it cannot cure the disease in the chronic phase (Agmon et al., 2018). Nifurtimox and benznidazole use can lead to cross-resistance. Besides, 30 % of adult individuals experience chronic Chagas infection with mega digestive syndromes and cardiomyopathy symptoms (Agmon et al., 2018). By sequence analysis, Trypanosoma cruzi ascorbate peroxidase falls under class 1 heme peroxidase, a member of a hybrid type A. for the establishment of the infection, parasite antioxidant systems are crucial (Arlian, Morgan and Rider, 2016). Catalase and selenium are enzymes capable of metabolizing hydrogen peroxide, are not found in Trypanosoma cruzi. Trypanosoma cruzi antioxidant defense system systems are different from their host. Biochemical and morphological changes occur during the Trypanosoma cruzi life cyc ...
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