Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/10642
Full metadata record
DC FieldValueLanguage
dc.contributor.authorBaldwin, Graham Sen
dc.contributor.authorBailey, Michael Fen
dc.contributor.authorShehan, B Philipen
dc.contributor.authorSims, Iouliaen
dc.contributor.authorNorton, Raymond Sen
dc.date.accessioned2015-05-16T00:09:47Z-
dc.date.available2015-05-16T00:09:47Z-
dc.date.issued2008-11-15en
dc.identifier.citationThe Biochemical Journal; 416(1): 77-84en
dc.identifier.govdoc18636967en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/10642en
dc.description.abstractTyrosine sulfation is a common modification of many proteins, and the ability to phosphorylate tyrosine residues is an intrinsic property of many growth-factor receptors. In the present study, we have utilized the peptide hormone CCK(8) (cholecystokinin), which occurs naturally in both sulfated and unsulfated forms, as a model to investigate the effect of tyrosine modification on metal-ion binding. The changes in absorbance and fluorescence emission on Fe(3+) binding indicated that tyrosine sulfation or phosphorylation increased the stoichiometry from 1 to 2, without greatly affecting the affinity (0.6-2.8 microM at pH 6.5). Measurement of Ca(2+) binding with a Ca(2+)-selective electrode revealed that phosphorylated CCK(8) bound two Ca(2+) ions. CCK(8) and sulfated CCK(8) each bound only one Ca(2+) ion with lower affinity. Binding of Ca(2+), Zn(2+) or Bi(3+) to phosphorylated CCK(8) did not cause any change in absorbance, but substantially increased the change in absorbance on subsequent addition of Fe(3+). The results of the present study demonstrate that tyrosine modification may increase the affinity of metal-ion binding to peptides, and imply that metal ions may directly regulate many signalling pathways.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherBismuth.metabolismen
dc.subject.otherCOS Cellsen
dc.subject.otherCalcium.metabolismen
dc.subject.otherCercopithecus aethiopsen
dc.subject.otherCholecystokinin.chemistry.metabolismen
dc.subject.otherFerric Compounds.metabolismen
dc.subject.otherHumansen
dc.subject.otherPeptide Fragments.chemistry.metabolismen
dc.subject.otherPhosphorylationen
dc.subject.otherReceptors, Cholecystokinin.metabolismen
dc.subject.otherSpectrometry, Fluorescenceen
dc.subject.otherTyrosine.analogs & derivatives.chemistry.metabolismen
dc.subject.otherZinc.metabolismen
dc.titleTyrosine modification enhances metal-ion binding.en
dc.typeJournal Articleen
dc.identifier.journaltitleThe Biochemical journalen
dc.identifier.affiliationThe University of Melbourne Department of Surgery, Austin Health, Heidelberg, Victoria 3084, Australiaen
dc.identifier.doi10.1042/BJ20081059en
dc.description.pages77-84en
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pubmed/18636967en
Appears in Collections:Journal articles

Files in This Item:
There are no files associated with this item.


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.