| pubmed-article:4355490 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4355490 | lifeskim:mentions | umls-concept:C0085368 | lld:lifeskim |
| pubmed-article:4355490 | lifeskim:mentions | umls-concept:C0521449 | lld:lifeskim |
| pubmed-article:4355490 | lifeskim:mentions | umls-concept:C1417088 | lld:lifeskim |
| pubmed-article:4355490 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:4355490 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:4355490 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:4355490 | pubmed:dateCreated | 1973-12-16 | lld:pubmed |
| pubmed-article:4355490 | pubmed:abstractText | Two isoenzymes of malate dehydrogenase (MDH) were demonstrated in plasmodia of Physarum polycephalum by polyacrylamide-gel electrophoresis. The more "cathodal" form was uniquely associated with mitochondria (M-MDH) and the other form was found in the soluble cytoplasm (S-MDH). The isoenzymes were separated by acetone fractionation of soluble plasmodial homogenates acidified to pH 5.0. The M-MDH was purified 201-fold by cetylpyridinium chloride treatment, fractionation with ammonium sulfate, gradient elution from sulfoethyl cellulose at pH 6.0, and Sephadex G-100 chromatography. The S-MDH was purified 155-fold by ammonium sulfate fractionation, diethylaminoethyl cellulose chromatography, gradient elution from sulfoethyl cellulose at pH 5.5, and Sephadex G-100 chromatography. The optimal cis-oxalacetate concentrations were 0.35 mM for M-MDH and 0.25 mM for S-MDH, and the optimal pH for both isoenzymes was 7.6 for oxalacetate reduction. The optimal l-malate concentrations were 5 mM for S-MDH and 6 mM for M-MDH, and both isoenzymes exhibited an optimal pH of 10.0 for L-malate oxidation. The Michaelis constants of S-MDH and M-MDH served to discriminate between the isoenzymes. The S-MDH was more heat-stable than the M-MDH. High concentrations of oxalacetate and malate inhibited S-MDH more than M-MDH. The isoenzymes were further distinguished by their utilization of analogues of nicotinamide adenine dinucleotide. Many properties of the Physarum isoenzymes were similar to those of more complex organisms, especially vertebrates. | lld:pubmed |
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| pubmed-article:4355490 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4355490 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4355490 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:4355490 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4355490 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:4355490 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:4355490 | pubmed:author | pubmed-author:HenneyH RHRJr | lld:pubmed |
| pubmed-article:4355490 | pubmed:author | pubmed-author:TeagueW MWM | lld:pubmed |
| pubmed-article:4355490 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4355490 | pubmed:volume | 116 | lld:pubmed |
| pubmed-article:4355490 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4355490 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4355490 | pubmed:pagination | 673-84 | lld:pubmed |
| pubmed-article:4355490 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:4355490 | pubmed:year | 1973 | lld:pubmed |
| pubmed-article:4355490 | pubmed:articleTitle | Purification and properties of cytoplasmic and mitochondrial malate dehydrogenases of Physarum polycephalum. | lld:pubmed |
| pubmed-article:4355490 | pubmed:publicationType | Journal Article | lld:pubmed |
