Isolation of an urate-binding protein by affinity chromatography

descriptionPublicationkeyboard_double_arrow_right Article 01 May 1982 Italy English Publisher:Springer Science and Business Media LLCJournal:Applied Biochemistry and Biotechnology, volume 7, pages 189-194 (issn: 0273-2289, eissn: 1559-0291,

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Authors: MAZZONI, MARIA ROSA; MARTINI, CLAUDIA; SEGNINI D; CIOMPI ML; LUCACCHINI, ANTONIO;

doi: 10.1007/bf02798296

pmid: 24234229

handle: 11568/172647

Isolation of an urate-binding protein by affinity chromatography

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Abstract

This paper describes an affinity chromatography procedure to purify an urate binding protein from human serum. The specific ligand was 8-amino-2,6-dihydroxypurine bound to Sepharose through the amino group. The specific elution was obtained with an uric acid or allopurinol solution. Electrophoretic analysis of the eluted protein shows a single sharp band with an α2-globulin mobility. Molecular weight, determined by gel filtration, is approximately 70,000 daltons.

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Italy

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University of Pisa
Italy

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