Literature DB >> 2597355

Purification of human serum amyloid P component (SAP) by calcium affinity chromatography.

T Mantovaara1, H Pertoft, J Porath.   

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.

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Year:  1989        PMID: 2597355

Source DB:  PubMed          Journal:  Biotechnol Appl Biochem        ISSN: 0885-4513            Impact factor:   2.431


  2 in total

1.  Immobilized metal ion affinity chromatography.

Authors:  T T Yip; T W Hutchens
Journal:  Mol Biotechnol       Date:  1994-04       Impact factor: 2.695

2.  On the association between amyloid fibrils and glycosaminoglycans; possible interactive role of Ca2+ and amyloid P-component.

Authors:  T Stenstad; J H Magnus; K Syse; G Husby
Journal:  Clin Exp Immunol       Date:  1993-10       Impact factor: 4.330

  2 in total

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