Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:9154935rdf:typepubmed:Citationlld:pubmed
pubmed-article:9154935lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:9154935lifeskim:mentionsumls-concept:C0040679lld:lifeskim
pubmed-article:9154935lifeskim:mentionsumls-concept:C0229671lld:lifeskim
pubmed-article:9154935lifeskim:mentionsumls-concept:C0026882lld:lifeskim
pubmed-article:9154935lifeskim:mentionsumls-concept:C0004015lld:lifeskim
pubmed-article:9154935lifeskim:mentionsumls-concept:C1280500lld:lifeskim
pubmed-article:9154935lifeskim:mentionsumls-concept:C0871161lld:lifeskim
pubmed-article:9154935pubmed:issue18lld:pubmed
pubmed-article:9154935pubmed:dateCreated1997-6-26lld:pubmed
pubmed-article:9154935pubmed:abstractTextMutations of the aspartic acid residue at position 63 of the N-lobe of human serum transferrin substantially alter the metal ion- and anion-binding properties of the protein. Substitution of serine, asparagine, glutamic acid, or alanine results in the loss of a key component of the interface in the interdomain cleft and the metal-binding ligand, aspartic acid, leading in all cases to an increased preference for NTA rather than carbonate as the "synergistic" anion relative to the wild-type protein. Excess bicarbonate is required to eliminate the NTA and obtain the "correct" visible spectrum. Carbonate replaces NTA via an intermediate. Blue shifts for the characteristic absorption band of each mutant show a range of effects on the Fe-O (Tyr) interaction. Titration with Co(III) yielded the molecular absorption coefficient for each mutant except D63A, where Co(III) appeared to oxidize the tyrosine residues and damage the ability of the mutant to bind metal. The chelator, Tiron, removes iron from hTF/2N with a simple saturation kinetic mode with respect to the ligand concentration. Chloride inhibits the release in an interesting manner: the effect is initially sharp and then levels off with a minimum k(obs) at [KCl] = 0.5 M. However, the reaction of the D63 mutants with Tiron results in the formation of the ternary complexes Fe-hTF/2N-Tiron. Significant red shifts for the characteristic absorption bands of these complexes suggest a different ligation of Tiron in the mutants from that in wild-type hTF/2N.lld:pubmed
pubmed-article:9154935pubmed:granthttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:languageenglld:pubmed
pubmed-article:9154935pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:citationSubsetIMlld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:9154935pubmed:statusMEDLINElld:pubmed
pubmed-article:9154935pubmed:monthMaylld:pubmed
pubmed-article:9154935pubmed:issn0006-2960lld:pubmed
pubmed-article:9154935pubmed:authorpubmed-author:WoodworthR...lld:pubmed
pubmed-article:9154935pubmed:authorpubmed-author:MacGillivrayR...lld:pubmed
pubmed-article:9154935pubmed:authorpubmed-author:L?tJJlld:pubmed
pubmed-article:9154935pubmed:authorpubmed-author:MasonA BABlld:pubmed
pubmed-article:9154935pubmed:authorpubmed-author:TanB LBLlld:pubmed
pubmed-article:9154935pubmed:authorpubmed-author:WadsworthTTlld:pubmed
pubmed-article:9154935pubmed:issnTypePrintlld:pubmed
pubmed-article:9154935pubmed:day6lld:pubmed
pubmed-article:9154935pubmed:volume36lld:pubmed
pubmed-article:9154935pubmed:ownerNLMlld:pubmed
pubmed-article:9154935pubmed:authorsCompleteYlld:pubmed
pubmed-article:9154935pubmed:pagination5522-8lld:pubmed
pubmed-article:9154935pubmed:dateRevised2011-11-17lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:meshHeadingpubmed-meshheading:9154935-...lld:pubmed
pubmed-article:9154935pubmed:year1997lld:pubmed
pubmed-article:9154935pubmed:articleTitleEffects of mutations of aspartic acid 63 on the metal-binding properties of the recombinant N-lobe of human serum transferrin.lld:pubmed
pubmed-article:9154935pubmed:affiliationDepartment of Biochemistry, College of Medicine, University of Vermont, Burlington 05405, USA. QHE@zoo.uvm.edulld:pubmed
pubmed-article:9154935pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9154935pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
pubmed-article:9154935pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:9154935lld:pubmed