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Model studies on iron (III) ion affinity chromatography: II. Interaction of immobilized ferric ions with phosphorylated amino acids, peptides and proteins
Polish Academy of Science, Warsawa. (Grazyna Muszynska)
Polish Academy of Science, Warsawa. (Grazyna Muszynska)
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - BMC, Biochemistry. (Jerker Porath)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology. (ek pia)
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1992 (English)In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 604, no 1, 19-28 p.Article in journal (Refereed) Published
Abstract [en]

The chromatographic behaviour of phosphoamino acids, phosphopeptides and phosphoproteins and their non-phosphorylated counterparts was studied on Fe(III)-Chelating Sepharose and Fe(III)-Chelating Superose. The phosphorylated compounds, in contrast to their non-phosphorylated or dephosphorylated counterparts, adsorb to immobilized iron(III) ions at pH 5.5 and can be desorbed by an increase in pH. Phosphoamino acids were eluted at pH 6.5-6.7, whereas monophosphopeptides and phosphoprotamine eluted in the pH range 6.9-7.5. Molecules possessing clusters(s) of carboxylic groups are weakly retained (gamma-carboxyglutamic acid, Ala-Ser-Glu5) or bound (polyglutamic acid, beta-casein) to the immobilized iron(III) ions at pH 5.5. Dephosphorylated beta-casein was desorbed at pH 7.0, whereas for elution of native (non-dephosphorylated) beta-casein, phosphate buffer of pH 7.7 was required. The homopolymer of polyglutamic acid was desorbed in the pH range 6.0-6.3, whereas copolymers of glutamic acid and tyrosine require pH 7.0-7.3 or even phosphate buffer at pH 7.7 for elution.

Place, publisher, year, edition, pages
1992. Vol. 604, no 1, 19-28 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:uu:diva-173132DOI: 10.1016/0021-9673(92)85524-WOAI: oai:DiVA.org:uu-173132DiVA: diva2:516703
Available from: 2012-04-19 Created: 2012-04-19 Last updated: 2012-04-19Bibliographically approved

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Ekman, Pia
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