• Title of article

    Comparison of protein A affinity sorbents: II. Mass transfer properties

  • Author/Authors

    Hahn، نويسنده , , Rainer and Bauerhansl، نويسنده , , Philipp and Shimahara، نويسنده , , Kazumichi and Wizniewski، نويسنده , , Christopher and Tscheliessnig، نويسنده , , Anne and Jungbauer، نويسنده , , Alois، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2005
  • Pages
    13
  • From page
    98
  • To page
    110
  • Abstract
    Protein A affinity chromatography is the standard purification method for isolation of therapeutic antibodies. Due to improvements in expression technology and optimization of fermentation, culture supernatants with high antibody content must be processed. Recently protein A affinity media with improved adsorption characteristics have been developed. The agarose media MabSelect Xtra and MabSelect SuRe are recent developments of the existing protein A affinity medium MabSelect. MabSelect Xtra is designed to exhibit a higher binding capacity for IgG, and MabSelect SuRe is functionalized with an alkaline stabilized protein A. ProSep-vA Ultra is a porous glass medium with a pore size of 70 nm, also developed to improve the binding capacity. Adsorption was measured in a finite and infinite bath. Mass transfer in these systems could be well described by a model including film and pore diffusion. Mass transfer parameters were used to accurately predict IgG breakthrough in packed bed mode. The dynamic binding capacity of all three media did not change when residence time was at least 4 min. All three media are suited for capture of feed stocks with high antibody content.
  • Keywords
    Staphylococcus protein A , Antibody , Film diffusion , Pore diffusion , Immunoglobulin
  • Journal title
    Journal of Chromatography A
  • Serial Year
    2005
  • Journal title
    Journal of Chromatography A
  • Record number

    1524564