By Miguel Castillo, Gerardo Hernández, Eduardo Sánchez, Tatiana Álvarez, Alexis Musacchio, Lorely Milá, Rubén López, Daily Hernández, Williams Ferro, Dobián Cecilia, Andrés Tamayo, José Montero, Regla Somoza, Tatiana González, Yurisleydis Aldama, Julio Valdés, José Marcelo, and Rodolfo Valdés
Volume 13, Issue 4 (Winter 2014/2015)
Immunoaffinity chromatography is an indispensable purification tool. However, its use has been limited by cost, purification cycle numbers, and storage requirements. Therefore, authors speculated that a possible solution to these problems could be CB.Hep-1 monoclonal antibody (mAb)-immunosorbent lyophilization. This study sought to assess the impact of the CB.Hep-1 mAb quantification by enzyme-linked immunoadsorbent assay and the CB.Hep-1 mAb-immunosorbent lyophilization process for its impact on hepatitis B virus surface antigen purification for pharmaceutical use. Study results found that CB.Hep-1 mAb lyophilization did not affect mAb purity and antigen recognition capacity. CB.Hep-1 mAb-immunosorbent lyophilization did not modify volume-weight factor, infrared spectrum, particle-size distribution, particle density and viscosity, antigen adsorption capacity, antigen elution capacity, antigen recovery, antigen purity, gamma immunoglobulin (IgG) leakage, and purification cycle number. Therefore, the lyophilized CB.Hep-1 mAb and CB.Hep-1 mAb-immunosorbents can be successfully used for hepatitis B vaccine production…
Citation: Castillo M et al. Characterization of a lyophilized immunoaffinity chromatography matrix employed to purify hepatitis B surface antigen for pharmaceutical use. BioProcess J, 2015; 13(4): 35–45. https://doi.org/10.12665/J134.Valdes
Posted online January 20, 2015