title: Purification of human serum amyloid P component (SAP) by calcium affinity chromatography.
abstract: Serum amyloid P component (SAP) has been purified from human serum by means of immobilized metal ion affinity chromatography (IMAC). It was selectively concentrated on carboxymethylated aspartic acid agarose (CM-Asp-agarose) loaded with calcium and, employing very mild conditions, purified to electrophoretical and immunological homogeneity in a single step amounting to about 1900-fold purification. As a purification method our procedure thus compares well with bio-specific affinity chromatography.
authors.affiliation: Institute of Biochemistry, University of Uppsala, Sweden.
authors.forename: T
authors.initials: T
authors.lastname: Mantovaara
authors.forename: H
authors.initials: H
authors.lastname: Pertoft
authors.forename: J
authors.initials: J
authors.lastname: Porath
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002118:Calcium; D002846:Chromatography, Affinity / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D011233:Precipitin Tests; D000683:Serum Amyloid P-Component / Q000302:isolation & purification*
chemical_list: D000596:Amino Acids; D000683:Serum Amyloid P-Component; D002118:Calcium