title: A new purification procedure for bovine C-reactive protein and serum amyloid P component.
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.
authors.affiliation: Department of Veterinary Science, National Institute of Health, Tokyo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Sarikaputi
authors.forename: M
authors.initials: M
authors.lastname: Morimatsu
authors.forename: B
authors.initials: B
authors.lastname: Syuto
authors.forename: M
authors.initials: M
authors.lastname: Saito
authors.forename: M
authors.initials: M
authors.lastname: Naiki
mesh_terms: D000818:Animals; D002097:C-Reactive Protein / Q000302:isolation & purification*; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D000683:Serum Amyloid P-Component / Q000302:isolation & purification*
chemical_list: D000683:Serum Amyloid P-Component; D002097:C-Reactive Protein