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A new purification procedure for bovine C-reactive protein and serum amyloid P component
M Sarikaputi1, M Morimatsu, B Syuto
1Department of Veterinary Science, National Institute of Health, Tokyo, Japan.
The International Journal of Biochemistry
|January 1, 1991
Abstract:
1. A new purification procedure was started with salting-out fractionation of serum proteins at 45-75% saturated ammonium sulfate concentration, followed by HE agarose affinity chromatography by which calcium-dependently bound CRP and SAP were purely eluted with EDTA-containing buffer. 2. Pure CRP and SAP were finally separated by DEAE-5PW HPLC. 3. This procedure gave recovery of 15 and 26%, and fold purification of 2650 and 2400 for CRP and SAP, respectively. 4. Each subunit of CRP and SAP had one intrasubunit disulfide bond, determined by reduction and carboxymethylation.