| pubmed-article:3325042 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3325042 | lifeskim:mentions | umls-concept:C0085467 | lld:lifeskim |
| pubmed-article:3325042 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:3325042 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:3325042 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:3325042 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:3325042 | lifeskim:mentions | umls-concept:C0064547 | lld:lifeskim |
| pubmed-article:3325042 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3325042 | pubmed:dateCreated | 1988-3-15 | lld:pubmed |
| pubmed-article:3325042 | pubmed:abstractText | L-Mandelate dehydrogenase was purified from Acinetobacter calcoaceticus by Triton X-100 extraction from a 'wall + membrane' fraction, ion-exchange chromatography on DEAE-Sephacel, (NH4)2SO4 fractionation and gel filtration followed by further ion-exchange chromatography. The purified enzyme was partially characterized with respect to its subunit Mr (44,000), pH optimum (7.5), pI value (4.2), substrate specificity and susceptibility to various potential inhibitors including thiol-blocking reagents. FMN was identified as the non-covalently bound cofactor. The properties of L-mandelate dehydrogenase are compared with those of D-mandelate dehydrogenase, D-lactate dehydrogenase and L-lactate dehydrogenase from A. calcoaceticus. | lld:pubmed |
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| pubmed-article:3325042 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3325042 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3325042 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3325042 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3325042 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3325042 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:3325042 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3325042 | pubmed:author | pubmed-author:FewsonC ACA | lld:pubmed |
| pubmed-article:3325042 | pubmed:author | pubmed-author:ScottA JAJ | lld:pubmed |
| pubmed-article:3325042 | pubmed:author | pubmed-author:AllisonNN | lld:pubmed |
| pubmed-article:3325042 | pubmed:author | pubmed-author:HoeyM EME | lld:pubmed |
| pubmed-article:3325042 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3325042 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3325042 | pubmed:volume | 248 | lld:pubmed |
| pubmed-article:3325042 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3325042 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3325042 | pubmed:pagination | 871-6 | lld:pubmed |
| pubmed-article:3325042 | pubmed:dateRevised | 2010-10-13 | lld:pubmed |
| pubmed-article:3325042 | pubmed:meshHeading | pubmed-meshheading:3325042-... | lld:pubmed |
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| pubmed-article:3325042 | pubmed:meshHeading | pubmed-meshheading:3325042-... | lld:pubmed |
| pubmed-article:3325042 | pubmed:meshHeading | pubmed-meshheading:3325042-... | lld:pubmed |
| pubmed-article:3325042 | pubmed:meshHeading | pubmed-meshheading:3325042-... | lld:pubmed |
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| pubmed-article:3325042 | pubmed:meshHeading | pubmed-meshheading:3325042-... | lld:pubmed |
| pubmed-article:3325042 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3325042 | pubmed:articleTitle | Purification and properties of L-mandelate dehydrogenase and comparison with other membrane-bound dehydrogenases from Acinetobacter calcoaceticus. | lld:pubmed |
| pubmed-article:3325042 | pubmed:affiliation | Department of Biochemistry, University of Glasgow, U.K. | lld:pubmed |
| pubmed-article:3325042 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3325042 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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