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Purification of human serum amyloid P component (SAP) by calcium affinity chromatography
Author(s) -
Mantovaara T.,
Pertoft H.,
Porath J.
Publication year - 1989
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1989.tb00073.x
Subject(s) - affinity chromatography , agarose , chromatography , chemistry , serum amyloid p component , ion chromatography , aspartic acid , calcium , biochemistry , enzyme , amino acid , biology , organic chemistry , c reactive protein , immunology , inflammation
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.