Isolation of an urate-binding protein by affinity chromatography.
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.
Department of Biochemistry and Service of Rheumatology, University of Pisa, Via Roma 55, 56100, Pisa, Italy.
M R
MR
Mazzoni
C
C
Martini
D
D
Segnini
M L
ML
Ciompi
A
A
Lucacchini