| pubmed-article:12416994 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C0034963 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C1510438 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C1709027 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C0444498 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C0077418 | lld:lifeskim |
| pubmed-article:12416994 | lifeskim:mentions | umls-concept:C0077419 | lld:lifeskim |
| pubmed-article:12416994 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:12416994 | pubmed:dateCreated | 2003-1-22 | lld:pubmed |
| pubmed-article:12416994 | pubmed:abstractText | Trypanothione reductase (TryR) is a key enzyme involved in the oxidative stress management of the Trypanosoma and Leishmania parasites, which helps to maintain an intracellular reducing environment by reduction of the small-molecular-mass disulphide trypanothione (T[S](2)) to its di-thiol derivative dihydrotrypanothione (T[SH](2)). TryR inhibition studies are currently impaired by the prohibitive costs of the native enzyme substrate T[S](2). Such costs are particularly notable in time-dependent and high-throughput inhibition assays. In the present study we report a protocol that greatly decreases the substrate quantities needed for such assays. This is achieved by coupling the assay with the chemical oxidant 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB), which can rapidly re-oxidize the T[SH](2) product back into the disulphide substrate T[S](2), thereby maintaining constant substrate concentrations and avoiding deviations from rate linearity due to substrate depletion. This has enabled the development of a continuous microplate assay for both classical and time-dependent TryR inhibition in which linear reaction rates can be maintained for 60 min or more using minimal substrate concentrations (<1 microM, compared with a substrate K (m) value of 30 microM) that would normally be completely consumed within seconds. In this manner, substrate requirements are decreased by orders of magnitude. The characterization of a novel time-dependent inhibitor, cis -3-oxo-8,9b-bis-(N(1)-acrylamidospermidyl)-1,2,3,4,4a,9b-hexahydrobenzofuran (PK43), is also described using these procedures. | lld:pubmed |
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| pubmed-article:12416994 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12416994 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12416994 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12416994 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12416994 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:12416994 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:12416994 | pubmed:author | pubmed-author:FairlambAlan... | lld:pubmed |
| pubmed-article:12416994 | pubmed:author | pubmed-author:HamiltonChris... | lld:pubmed |
| pubmed-article:12416994 | pubmed:author | pubmed-author:Saravanamuthu... | lld:pubmed |
| pubmed-article:12416994 | pubmed:author | pubmed-author:EgglestonIan... | lld:pubmed |
| pubmed-article:12416994 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12416994 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12416994 | pubmed:volume | 369 | lld:pubmed |
| pubmed-article:12416994 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12416994 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12416994 | pubmed:pagination | 529-37 | lld:pubmed |
| pubmed-article:12416994 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:12416994 | pubmed:meshHeading | pubmed-meshheading:12416994... | lld:pubmed |
| pubmed-article:12416994 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12416994 | pubmed:articleTitle | Ellman's-reagent-mediated regeneration of trypanothione in situ: substrate-economical microplate and time-dependent inhibition assays for trypanothione reductase. | lld:pubmed |
| pubmed-article:12416994 | pubmed:affiliation | Division of Biological Chemistry & Molecular Microbiology, School of Life Sciences, Carnelley Building, University of Dundee, Dundee DD1 4HN, UK. | lld:pubmed |
| pubmed-article:12416994 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12416994 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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