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Purification of polyclonal antibodies from Cohn fraction II + III, skim milk, and whey by affinity chromatography using a hexamer peptide ligand

Authors

  • Stefano Menegatti,

  • Amith D. Naik,

  • Patrick V. Gurgel,

  • Ruben G. Carbonell

    Corresponding author
    • Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC, USA
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Correspondence: Dr. Ruben G. Carbonell, Department of Chemical and Biomolecular Engineering, North Carolina State University, 911 Partners Way, Raleigh, North Carolina 27695-7905, USA

E-mail: ruben@ncsu.edu

Fax: +1-919-515-5831

Abstract

HWRGWV, a peptide that binds specifically to the Fc fragment of human immunoglobulin G (IgG), was used for the purification of IgG from Cohn fraction II + III of human plasma and from bovine skim milk and whey. The concentration of sodium chloride and sodium caprylate in the binding buffer as well as the pH of the elution buffer were optimized to achieve high IgG yield and purity. Under optimized conditions, IgG was recovered from plasma fractions with yield and purity up to 84% and 95%, respectively. IgG was also purified from skim milk with 74% yield and 92% purity and from whey with 85% yield and 93% purity. Purification experiments were also performed with Protein A resin and the results were found to be similar to those obtained with the peptide adsorbent.

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