Pharmaceutica Analytica Acta

Déborah Geada

Publications

• Research Article
  Significant Improvements in the Performance of an Established Affinity Chromatography Procedure Employed to Purify a Monoclonal Antibody in 100 Purification Cycles
  Author(s): Williams Ferro, Rodolfo Valdés, Eutimio Fernández, Yarysel Guevara, Yenisley Medina, Tatiana Álvarez, Andrés Tamayo, Tatiana González, Mayra Wood, Maylín La O, Yodelvis Calvo and Déborah GeadaWilliams Ferro, Rodolfo Valdés, Eutimio Fernández, Yarysel Guevara, Yenisley Medina, Tatiana Álvarez, Andrés Tamayo, Tatiana González, Mayra Wood, Maylín La O, Yodelvis Calvo and Déborah Geada
  
  Protein A-Sepharose affinity chromatography is a very successful method for the purification of immunoglobulins for pharmaceutical use. However, the chromatography efficiency and lifetime of this method have to be always adjusted to specific chromatography conditions (biological source, buffers, flow rates, antibody properties, temperature, protein concentration, cleaning protocol, etc). This study sought to demonstrate improvements in the performance of an established affinity chromatography procedure employed to purify the CB.Hep-1 monoclonal antibody (mAb) used in the purification of the active pharmaceutical ingredient of a Hepatitis B vaccine. In conclusion, the relative poor mAb recovery observed in 150 mM PBS; pH 8.0/100 mM citric acid; pH 3.0 buffer system conditions was attributed to the inefficacy of the elution buffer to disrupt completely interactions between the matrix an.. View More»
  DOI: 10.4172/2153-2435.1000143

  Abstract PDF