| pubmed-article:697734 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:697734 | lifeskim:mentions | umls-concept:C0009629 | lld:lifeskim |
| pubmed-article:697734 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:697734 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:697734 | pubmed:dateCreated | 1978-11-18 | lld:pubmed |
| pubmed-article:697734 | pubmed:abstractText | 1. The distribution of iron between the two iron-binding sites in partially saturated ovotransferrin was studied by labelling with 55Fe and 59Fe and by gel electrophoresis in a urea-containing buffer. 2. When iron is added in the form of chelate complexes at alkaline pH, binding occurs preferentially at the N-terminal binding site. In acid, binding occurs preferentially at the C-terminal site. 3. When simple iron donors (ferric and ferrous salts) are used the metal is distributed at random between the binding sites, as judged by the gel-electrophoresis method. The double-isotope method shows a preference of ferrous salts for the N-terminal site. 4. Quantitative treatment of the results of double-isotope labelling suggests that in the binding of iron to ovotransferrin at alkaline pH co-operative interactions between the sites occur. These interactions are apparently absent in the displacement of copper and in the binding of iron at acid pH. | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:language | eng | lld:pubmed |
| pubmed-article:697734 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:697734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:697734 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:697734 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:697734 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:697734 | pubmed:author | pubmed-author:WilliamsJJ | lld:pubmed |
| pubmed-article:697734 | pubmed:author | pubmed-author:EvansR WRW | lld:pubmed |
| pubmed-article:697734 | pubmed:author | pubmed-author:MoretonKK | lld:pubmed |
| pubmed-article:697734 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:697734 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:697734 | pubmed:volume | 173 | lld:pubmed |
| pubmed-article:697734 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:697734 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:697734 | pubmed:pagination | 533-39 | lld:pubmed |
| pubmed-article:697734 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-I... | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-I... | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-P... | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-B... | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-E... | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-C... | lld:pubmed |
| pubmed-article:697734 | pubmed:meshHeading | pubmed-meshheading:697734-E... | lld:pubmed |
| pubmed-article:697734 | pubmed:year | 1978 | lld:pubmed |
| pubmed-article:697734 | pubmed:articleTitle | The iron-binding properties of hen ovotransferrin. | lld:pubmed |
| pubmed-article:697734 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:697734 | lld:pubmed |
