| pubmed-article:3128167 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3128167 | lifeskim:mentions | umls-concept:C0023861 | lld:lifeskim |
| pubmed-article:3128167 | lifeskim:mentions | umls-concept:C0007367 | lld:lifeskim |
| pubmed-article:3128167 | lifeskim:mentions | umls-concept:C0332685 | lld:lifeskim |
| pubmed-article:3128167 | lifeskim:mentions | umls-concept:C1151619 | lld:lifeskim |
| pubmed-article:3128167 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3128167 | pubmed:dateCreated | 1988-5-10 | lld:pubmed |
| pubmed-article:3128167 | pubmed:abstractText | Four strains of Listeria monocytogenes were examined for catalase (CA) and superoxide dismutase (SOD) activities. The two strains having the highest CA activities (LCDC and Scott A) also possessed the highest SOD activities. The CA activity of heated cell extracts of all four strains examined decreased sharply between 55 and 60 degrees C. SOD was more heat labile than CA. Two L. monocytogenes strains demonstrated a decline in SOD activity after heat treatment at 45 degrees C, whereas the other two strains demonstrated a decline at 50 degrees C. Sublethal heating of the cells at 55 degrees C resulted in increased sensitivity to 5.5% NaCl. Exogenous hydrogen peroxide was added to suspensions of L. monocytogenes; strains producing the highest CA levels showed the greatest H2O2 resistance. | lld:pubmed |
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| pubmed-article:3128167 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3128167 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3128167 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3128167 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:3128167 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3128167 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:3128167 | pubmed:issn | 0099-2240 | lld:pubmed |
| pubmed-article:3128167 | pubmed:author | pubmed-author:MartinS ESE | lld:pubmed |
| pubmed-article:3128167 | pubmed:author | pubmed-author:DallmierA WAW | lld:pubmed |
| pubmed-article:3128167 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3128167 | pubmed:volume | 54 | lld:pubmed |
| pubmed-article:3128167 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3128167 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3128167 | pubmed:pagination | 581-2 | lld:pubmed |
| pubmed-article:3128167 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:3128167 | pubmed:meshHeading | pubmed-meshheading:3128167-... | lld:pubmed |
| pubmed-article:3128167 | pubmed:meshHeading | pubmed-meshheading:3128167-... | lld:pubmed |
| pubmed-article:3128167 | pubmed:meshHeading | pubmed-meshheading:3128167-... | lld:pubmed |
| pubmed-article:3128167 | pubmed:meshHeading | pubmed-meshheading:3128167-... | lld:pubmed |
| pubmed-article:3128167 | pubmed:meshHeading | pubmed-meshheading:3128167-... | lld:pubmed |
| pubmed-article:3128167 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3128167 | pubmed:articleTitle | Catalase and superoxide dismutase activities after heat injury of Listeria monocytogenes. | lld:pubmed |
| pubmed-article:3128167 | pubmed:affiliation | Department of Food Science, University of Illinois, Urbana 61801. | lld:pubmed |
| pubmed-article:3128167 | pubmed:publicationType | Journal Article | lld:pubmed |
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