by Déborah Geada, Aniel Sánchez, Vladimir Besada, Rodolfo Valdés, Lázaro Betancourt, Yasser Ramos, Yanet Támbara, Liudys García, Jeovanis Gil, Luis Javier González, Sigifredo Padilla, William Ferro, Leonardo Gómez, Andrés Tamayo, Otto Mendoza, and Carlos Borroto
Volume 6, Issue 2 (Summer 2007)
Regulatory agencies such as the FDA require the structure and amino acid sequence characterization of recombinant monoclonal antibodies (MAbs) to grant marketing approval. Characterizing such complex, inherently heterogeneous molecules is a significant analytical challenge that requires a broad array of physicochemical tests. Mass spectrometry (MS) is an essential tool for characterizing protein identity, functions, substrate specificity and amino acid sequence (AAS) of recombinant MAb biotherapeutics as it complements, or in some cases supersedes the utility of traditional biological methods. For some of the most important proteomic applications, the high sensitivity and accuracy provided by modern MS has allowed the unequivocal protein characterization…
Citation:
Geada D et al. An Investigative Comparison: Plant-Based MAbs for Hep B Surface Antigen and MAbs from Mice. BioProcess J, 2007; 6(2): 8-13. http://dx.doi.org/10.12665/J62.Geada