CAMPERI Silvia Andrea
Monoclonal antibody purification by affinity chromatography with ligands derived from the screening of peptide combinatory libraries
SILVIA A. CAMPERI; NANCY B. IANNUCCI; GUILLERMO J. ALBANESI; MARCOS OGGERO EBERHARDT; MARINA ETCHEVERRIGARAY; ANGEL MESSEGUER; FERNANDO ALBERICIO; OSVALDO CASCONE
Kluwer Academic Publishers
Año: 2003 vol. 25 p. 1545 - 1545
The peptide, Ala-Pro-Ala-Arg (APAR), was selected from the screening of a tetrapeptide combinatorial synthetic library as the ligand for affinity purification of an anti-Granulocyte Macrophage-Colony Stimulating Factor (GMCSF) monoclonal antibody (Mab) developed in mouse ascitis. The affinity chromatographic matrix obtained by attachment of APAR to agarose, having a peptide density of 0.5 µmolml−1, showed a maximum capacity of 9.1mg Mab ml−1 and a dynamic capacity of 3.9 mg Mab ml−1. A 95% yield of electrophoretically pure anti-GM-CSF was obtained in a single step.