One-step purification of vitronectin from human plasma by affinity chromatography on phage-displayed peptides. | Zendy

Szymon Skurzyński | Zendy

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One-step purification of vitronectin from human plasma by affinity chromatography on phage-displayed peptides.

Author(s) -

Szymon Skurzyński

Publication year - 2010

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2010_2377

Subject(s) - vitronectin , affinity chromatography , chemistry , chromatography , human plasma , sepharose , elution , ligand (biochemistry) , phage display , covalent bond , biochemistry , peptide , receptor , enzyme , integrin , organic chemistry

A novel affinity purification method for rapid isolation of vitronectin (VN) from human plasma is described. Recently we have used phage display technology to obtain clones expressing peptides with high binding activity for VN. The isolated "strong VN binders" were covalently coupled to CNBr-activated Sepharose. Human plasma was applied to the column and bound VN was eluted using 0.5 M acetic acid, giving purity exceeding 90%. The developed method is a convenient alternative to conventional antibody-antigen affinity chromatography techniques for purification of VN, as it offers low ligand cost, is rapid and ensures good protein recovery from human plasma.

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