Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/9733
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dc.contributor.authorBaldwin, Graham Sen
dc.date.accessioned2015-05-15T22:56:05Z-
dc.date.available2015-05-15T22:56:05Z-
dc.date.issued2004-01-01en
dc.identifier.citationThe Protein Journal; 23(1): 65-70en
dc.identifier.govdoc15115183en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/9733en
dc.description.abstractBinding of ferric ions to the hormone glycine-extended gastrin17 is essential for biological activity (Pannequin, J., et al. (2002). J. Biol. Chem. 277: 48602-48609). The aims of the current study were to determine the properties of the complex between recombinant human progastrin6-80 and ferric ions. The stoichiometry and affinity of ferric ion binding were determined by fluorescence spectroscopy. The selectivity of metal ion binding and the stability of the 59Fe(III) progastrin6-80 complex were determined by equilibrium dialysis. The stoichiometry of 2.5 +/- 0.1 moles Fe/mole progastrin, and the apparent dissociation constant of 2.2 +/- 0.1 microM, were similar to the values previously determined for glycine-extended gastrin17 at pH 4.0. Of the four trivalent and seven divalent metal ions tested, only ferrous and ferric ions bound to progastrin6-80. The ferric ion-progastrin complex was extremely stable, with a half-life of 117 +/- 8 days at pH 7.6 and 25 degrees C. We conclude that recombinant human progastrin6-80 selectively binds ferrous and ferric ions with high affinity in a stable 2:1 complex.en
dc.language.isoenen
dc.subject.otherBinding Sitesen
dc.subject.otherFerric Compounds.chemistry.metabolismen
dc.subject.otherGastrins.chemistry.genetics.metabolismen
dc.subject.otherHumansen
dc.subject.otherKineticsen
dc.subject.otherProtein Bindingen
dc.subject.otherProtein Precursors.chemistry.genetics.metabolismen
dc.subject.otherRecombinant Proteins.chemistry.genetics.metabolismen
dc.titleProperties of the complex between recombinant human progastrin and ferric ions.en
dc.typeJournal Articleen
dc.identifier.journaltitleThe protein journalen
dc.identifier.affiliationUniversity of Melbourne, Department of Surgery, Austin Campus, Austin, Australiaen
dc.description.pages65-70en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/15115183en
dc.type.austinJournal Articleen
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairetypeJournal Article-
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