Investigating the Novel Redox Active Thioredoxin-like Protein (PbTrxL-1) of the Malaria Parasite Plasmodium
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MLA citation style (9th ed.)
Investigating the Novel Redox Active Thioredoxin-like Protein (pbtrxl-1) of the Malaria Parasite Plasmodium. . 1192. marian.hykucommons.org/concern/generic_works/d1480764-9302-4061-b392-d1d87c31f517.APA citation style (7th ed.)
(1192). Investigating the Novel Redox Active Thioredoxin-like Protein (PbTrxL-1) of the Malaria Parasite Plasmodium. https://marian.hykucommons.org/concern/generic_works/d1480764-9302-4061-b392-d1d87c31f517Chicago citation style (CMOS 17, author-date)
Investigating the Novel Redox Active Thioredoxin-Like Protein (pbtrxl-1) of the Malaria Parasite Plasmodium. 1192. https://marian.hykucommons.org/concern/generic_works/d1480764-9302-4061-b392-d1d87c31f517.Note: These citations are programmatically generated and may be incomplete.
Redox systems are an important component of the cellular metabolism. We have characterized a novel thioredoxin-like protein (TrxL-1) of the malaria parasite Plasmodium and have previously determined that the trxl-1 gene is specifically expressed during development of rodent malaria model parasite Plasmodium berghei in its mosquito vector. Here I describe the optimization of recombinant TrxL-1 expression and subsequent purification under denaturing conditions. Using biochemical assays, I demonstrate that TrxL-1 is redox active with the Plasmodium thioredoxin system. Recent reports have shown that in Toxoplasma gondii, a related species, the homologous TrxL-1 interacts with SAXO-1 which plays an important role in the regulation of microtubules. The Plasmodium homolog of SAXO-1 and its interaction with TrxL-1 is currently under investigation in our lab.
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