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

100%

Skurzynski S.

Acta Biochimica Polonica

2010

tom 57

nr 1

89-93

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.

In vivo imaging using liposomal phage display peptide derivates targeting integrins in activated leucocytes

100%

Ranta T. M., Valtanen H., Kaukinen S., Boerman O. C., Simpura I., Zhu Y., Medina O. P., Oyen W. J. G., Kairemo K.

Cellular and Molecular Biology Letters

2005

tom 10

nr Suppl.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Cellular and Molecular Biology Letters

1 Boerman O. C.

1 Kairemo K.

1 Kaukinen S.

1 Medina O. P.

1 Oyen W. J. G.

1 Ranta T. M.

1 Simpura I.

1 Skurzynski S.

1 Valtanen H.

1 Zhu Y.

1 2010

1 2005

Wyniki wyszukiwania

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

In vivo imaging using liposomal phage display peptide derivates targeting integrins in activated leucocytes