| pubmed-article:11535129 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0040549 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0030011 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0036451 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0549193 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0392760 | lld:lifeskim |
| pubmed-article:11535129 | lifeskim:mentions | umls-concept:C0536054 | lld:lifeskim |
| pubmed-article:11535129 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:11535129 | pubmed:dateCreated | 2001-9-5 | lld:pubmed |
| pubmed-article:11535129 | pubmed:abstractText | Maurotoxin (MTX) is a 34-mer scorpion toxin cross-linked by four disulphide bridges that acts on various K(+) channel subtypes. MTX adopts a disulphide bridge organization of the type C1-C5, C2-C6, C3-C4 and C7-C8, and folds according to the common alpha/beta scaffold reported for other known scorpion toxins. Here we have investigated the process and kinetics of the in vitro oxidation/folding of reduced synthetic L-MTX (L-sMTX, where L-MTX contains only L-amino acid residues). During the oxidation/folding of reduced L-sMTX, the oxidation intermediates were blocked by iodoacetamide alkylation of free cysteine residues, and analysed by MS. The L-sMTX intermediates appeared sequentially over time from the least (intermediates with one disulphide bridge) to the most oxidized species (native-like, four-disulphide-bridged L-sMTX). The mathematical formulation of the diffusion-collision model being inadequate to accurately describe the kinetics of oxidation/folding of L-sMTX, we have formulated a derived mathematical description that better fits the experimental data. Using this mathematical description, we have compared for the first time the oxidation/folding of L-sMTX with that of D-sMTX, its stereoisomer that contains only D-amino acid residues. Several experimental parameters, likely to affect the oxidation/folding process, were studied further; these included temperature, pH, ionic strength, redox potential and concentration of reduced toxin. We also assessed the effects of some cellular enzymes, peptidylprolyl cis-trans isomerase (PPIase) and protein disulphide isomerase (PDI), on the folding pathways of reduced L-sMTX and D-sMTX. All the parameters tested affect the oxidative folding of sMTX, and the kinetics of this process were indistinguishable for L-sMTX and D-sMTX, except when stereospecific enzymes were used. The most efficient conditions were found to be: 50 mM Tris/HCl/1.4 mM EDTA, pH 7.5, supplemented by 0.5 mM PPIase and 50 units/ml PDI for 0.1 mM reduced compound. These data represent the first report of potent stereoselective effects of cellular enzymes on the oxidation/folding of a scorpion toxin. | lld:pubmed |
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| pubmed-article:11535129 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11535129 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11535129 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11535129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11535129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11535129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11535129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11535129 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11535129 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11535129 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:11535129 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:RochatHH | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:SandowDD | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:EstèveEE | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:De WaardMM | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:MansuellePP | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:SabatierJ MJM | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:FathallahMM | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:KharratRR | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:FajlounZZ | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:di LuccioEE | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:RegayaII | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:CarregaLL | lld:pubmed |
| pubmed-article:11535129 | pubmed:author | pubmed-author:AzulayD ODO | lld:pubmed |
| pubmed-article:11535129 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11535129 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11535129 | pubmed:volume | 358 | lld:pubmed |
| pubmed-article:11535129 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11535129 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11535129 | pubmed:pagination | 681-92 | lld:pubmed |
| pubmed-article:11535129 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:11535129 | pubmed:meshHeading | pubmed-meshheading:11535129... | lld:pubmed |
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| pubmed-article:11535129 | pubmed:meshHeading | pubmed-meshheading:11535129... | lld:pubmed |
| pubmed-article:11535129 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11535129 | pubmed:articleTitle | Parameters affecting in vitro oxidation/folding of maurotoxin, a four-disulphide-bridged scorpion toxin. | lld:pubmed |
| pubmed-article:11535129 | pubmed:affiliation | CNRS UMR 6560, Bd Pierre Dramard, 13916 Marseille Cedex 20, France. | lld:pubmed |
| pubmed-article:11535129 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11535129 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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