| pubmed-article:1497609 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1497609 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1497609 | lifeskim:mentions | umls-concept:C0040679 | lld:lifeskim |
| pubmed-article:1497609 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
| pubmed-article:1497609 | lifeskim:mentions | umls-concept:C0243144 | lld:lifeskim |
| pubmed-article:1497609 | lifeskim:mentions | umls-concept:C2346726 | lld:lifeskim |
| pubmed-article:1497609 | pubmed:dateCreated | 1992-9-10 | lld:pubmed |
| pubmed-article:1497609 | pubmed:abstractText | We have studied the binding of Al3+ to human serum apotransferrin (80 kDa) and recombinant N-lobe human apotransferrin (40 kDa) in 0.1 M-sodium bicarbonate solution at a pH meter reading in 2H2O (pH*) of 8.8 using 1H n.m.r. spectroscopy. The results show that for the intact protein, preferential binding of Al3+ to the N-lobe occurs. Molecular modelling combined with an analysis of ring-current-induced shifts suggest that n.m.r. spectroscopy can be used to probe hinge bending processes which accompany metal uptake in solution. | lld:pubmed |
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| pubmed-article:1497609 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1497609 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1497609 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1497609 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1497609 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1497609 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1497609 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:1497609 | pubmed:author | pubmed-author:TuckerAA | lld:pubmed |
| pubmed-article:1497609 | pubmed:author | pubmed-author:SadlerP JPJ | lld:pubmed |
| pubmed-article:1497609 | pubmed:author | pubmed-author:WoodworthR... | lld:pubmed |
| pubmed-article:1497609 | pubmed:author | pubmed-author:KubaiDD | lld:pubmed |
| pubmed-article:1497609 | pubmed:author | pubmed-author:MasonA BAB | lld:pubmed |
| pubmed-article:1497609 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1497609 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:1497609 | pubmed:volume | 285 ( Pt 3) | lld:pubmed |
| pubmed-article:1497609 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1497609 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1497609 | pubmed:pagination | 711-4 | lld:pubmed |
| pubmed-article:1497609 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:1497609 | pubmed:meshHeading | pubmed-meshheading:1497609-... | lld:pubmed |
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| pubmed-article:1497609 | pubmed:meshHeading | pubmed-meshheading:1497609-... | lld:pubmed |
| pubmed-article:1497609 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1497609 | pubmed:articleTitle | Uptake of Al3+ into the N-lobe of human serum transferrin. | lld:pubmed |
| pubmed-article:1497609 | pubmed:affiliation | Department of Chemistry, Birkbeck College, University of London, U.K. | lld:pubmed |
| pubmed-article:1497609 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1497609 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1497609 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1497609 | lld:pubmed |
