Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/9733
Title: Properties of the complex between recombinant human progastrin and ferric ions.
Authors: Baldwin, Graham S
Affiliation: University of Melbourne, Department of Surgery, Austin Campus, Austin, Australia. grahamsb@unimelb.edu.au
Issue Date: 1-Jan-2004
Citation: The Protein Journal; 23(1): 65-70
Abstract: Binding 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.
Internal ID Number: 15115183
URI: http://ahro.austin.org.au/austinjspui/handle/1/9733
URL: http://www.ncbi.nlm.nih.gov/pubmed/15115183
Type: Journal Article
Subjects: Binding Sites
Ferric Compounds.chemistry.metabolism
Gastrins.chemistry.genetics.metabolism
Humans
Kinetics
Protein Binding
Protein Precursors.chemistry.genetics.metabolism
Recombinant Proteins.chemistry.genetics.metabolism
Appears in Collections:Journal articles

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