pubmed-article:10417186 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10417186 | lifeskim:mentions | umls-concept:C0026926 | lld:lifeskim |
pubmed-article:10417186 | lifeskim:mentions | umls-concept:C0027021 | lld:lifeskim |
pubmed-article:10417186 | lifeskim:mentions | umls-concept:C0015264 | lld:lifeskim |
pubmed-article:10417186 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:10417186 | pubmed:issue | 8 | lld:pubmed |
pubmed-article:10417186 | pubmed:dateCreated | 1999-8-12 | lld:pubmed |
pubmed-article:10417186 | pubmed:abstractText | We investigated the antimycobacterial role of myeloperoxidase (MPO), one of the most abundant granule proteins in human neutrophils. Our data indicate that purified MPO, in the presence of hydrogen peroxide, exerts a consistent killing activity against Mycobacterium tuberculosis H37Rv and against a clinical isolate. The activity is time and dose dependent and requires the presence of chloride ions in the assay medium. | lld:pubmed |
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pubmed-article:10417186 | pubmed:language | eng | lld:pubmed |
pubmed-article:10417186 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10417186 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10417186 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10417186 | pubmed:month | Aug | lld:pubmed |
pubmed-article:10417186 | pubmed:issn | 0019-9567 | lld:pubmed |
pubmed-article:10417186 | pubmed:author | pubmed-author:ZabucchiGG | lld:pubmed |
pubmed-article:10417186 | pubmed:author | pubmed-author:BanfiEE | lld:pubmed |
pubmed-article:10417186 | pubmed:author | pubmed-author:BorelliVV | lld:pubmed |
pubmed-article:10417186 | pubmed:author | pubmed-author:PerrottaM GMG | lld:pubmed |
pubmed-article:10417186 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10417186 | pubmed:volume | 67 | lld:pubmed |
pubmed-article:10417186 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10417186 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10417186 | pubmed:pagination | 4149-52 | lld:pubmed |
pubmed-article:10417186 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:10417186 | pubmed:meshHeading | pubmed-meshheading:10417186... | lld:pubmed |
pubmed-article:10417186 | pubmed:meshHeading | pubmed-meshheading:10417186... | lld:pubmed |
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pubmed-article:10417186 | pubmed:meshHeading | pubmed-meshheading:10417186... | lld:pubmed |
pubmed-article:10417186 | pubmed:meshHeading | pubmed-meshheading:10417186... | lld:pubmed |
pubmed-article:10417186 | pubmed:meshHeading | pubmed-meshheading:10417186... | lld:pubmed |
pubmed-article:10417186 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10417186 | pubmed:articleTitle | Myeloperoxidase exerts microbicidal activity against Mycobacterium tuberculosis. | lld:pubmed |
pubmed-article:10417186 | pubmed:affiliation | Dipartimento di Fisiologia e Patologia, Università di Trieste, 34127 Trieste, Italy. | lld:pubmed |
pubmed-article:10417186 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10417186 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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