| pubmed-article:36074 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:36074 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:36074 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:36074 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:36074 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:36074 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:36074 | lifeskim:mentions | umls-concept:C0072435 | lld:lifeskim |
| pubmed-article:36074 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:36074 | pubmed:dateCreated | 1979-7-25 | lld:pubmed |
| pubmed-article:36074 | pubmed:abstractText | The effects of pH and Ca2+ on the intrinsic fluorescence of bovine prothrombin fragment 1 were investigated to deduce the nature of protein functional groups involved in Ca2+ binding to fragment 1. From pH values of 9 to 3, increasing the H3O+ concentration results in quenching of the fluorescence of fragment 1. Reversible pH-titration curves are obtained which appear to consist of two regions. From pH 4 to pH6.5 a broad titration curve is obtained, whereas from pH6.5 to 9 a more pronounced titration behaviour is evidenced by a group or groups on fragment 1 with an apparent pKa of approx. 7.5. In contrast, the apparent association constant for Ca2+ and fragment 1 shows a sharp pH-dependence in the region between pH7 and 8 with tighter Ca2+ binding at higher pH values. A PKa of approx. 7.5 can be estimated for the group or groups on fragment 1 linked to the tight binding of Ca2+. Both H3O+ and Ca2+ result in blue-shifts in the wave-lengths of fragment-1 emission. These results are interpreted in terms of H+ - and Ca2+ - induced changes in the conformation of fragment 1 as a result of surface-charge neutralization. | lld:pubmed |
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| pubmed-article:36074 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:36074 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:36074 | pubmed:language | eng | lld:pubmed |
| pubmed-article:36074 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:36074 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:36074 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:36074 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:36074 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:36074 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:36074 | pubmed:author | pubmed-author:KoehlerK AKA | lld:pubmed |
| pubmed-article:36074 | pubmed:author | pubmed-author:HiskeyR GRG | lld:pubmed |
| pubmed-article:36074 | pubmed:author | pubmed-author:ScottM EME | lld:pubmed |
| pubmed-article:36074 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:36074 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:36074 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:36074 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:36074 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:36074 | pubmed:pagination | 879-86 | lld:pubmed |
| pubmed-article:36074 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:36074 | pubmed:meshHeading | pubmed-meshheading:36074-An... | lld:pubmed |
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| pubmed-article:36074 | pubmed:meshHeading | pubmed-meshheading:36074-Sp... | lld:pubmed |
| pubmed-article:36074 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:36074 | pubmed:articleTitle | The effects of calcium ions and pH on bovine prothrombin fragment 1. Intrinsic fluroescence studies. | lld:pubmed |
| pubmed-article:36074 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:36074 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:36074 | lld:pubmed |
