| pubmed-article:8260935 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8260935 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8260935 | lifeskim:mentions | umls-concept:C0063146 | lld:lifeskim |
| pubmed-article:8260935 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8260935 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8260935 | lifeskim:mentions | umls-concept:C0147003 | lld:lifeskim |
| pubmed-article:8260935 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8260935 | pubmed:dateCreated | 1994-1-25 | lld:pubmed |
| pubmed-article:8260935 | pubmed:abstractText | When bovine serum albumin was exposed to the hydroxyl radical generating system of ascorbate-EDTA-Fe3+ or ascorbate-EDTA-Fe(3+)-H2O2, carbonyl formation occurred. Trolox strongly inhibited the oxidative modification in a dose-dependent manner. The fragmentation and enhancement of the proteolytic susceptibility of bovine serum albumin were induced by HO. only in the presence of O2, while trolox protected the protein against such oxidative modifications. In addition, inactivations of lactate dehydrogenase and creatine kinase induced by the hydroxyl radical were also blocked by trolox. | lld:pubmed |
| pubmed-article:8260935 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8260935 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260935 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8260935 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8260935 | pubmed:issn | 1039-9712 | lld:pubmed |
| pubmed-article:8260935 | pubmed:author | pubmed-author:OgisoTT | lld:pubmed |
| pubmed-article:8260935 | pubmed:author | pubmed-author:MiuraTT | lld:pubmed |
| pubmed-article:8260935 | pubmed:author | pubmed-author:MuraokaSS | lld:pubmed |
| pubmed-article:8260935 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8260935 | pubmed:volume | 31 | lld:pubmed |
| pubmed-article:8260935 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8260935 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8260935 | pubmed:pagination | 125-33 | lld:pubmed |
| pubmed-article:8260935 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
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| pubmed-article:8260935 | pubmed:meshHeading | pubmed-meshheading:8260935-... | lld:pubmed |
| pubmed-article:8260935 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8260935 | pubmed:articleTitle | Inhibition of hydroxyl radical-induced protein damages by trolox. | lld:pubmed |
| pubmed-article:8260935 | pubmed:affiliation | Department of Biochemistry, Hokkaido Institute of Pharmaceutical Sciences, Otaru, Japan. | lld:pubmed |
| pubmed-article:8260935 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8260935 | lld:pubmed |
