Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1176774 | Analytical Biochemistry | 2006 | 16 Pages |
Abstract
A therapeutic recombinant monoclonal antibody analyzed by cation-exchange chromatography exhibited a heterogeneous profile composed of approximately 10 isoforms. The peaks were isolated and characterized by electrospray quadrupole time-of-flight mass spectrometry (ESI-q-TOF–MS), N-terminal Edman sequencing, peptide mapping, and other techniques. Acidic (lower pI) peaks were found to represent deamidated and sialyated species. Higher pI peaks were found to contain N- and C-terminal heavy-chain variants. Biological activities of the more abundant isoforms were found to be comparable. An approach streamlining the characterization of antibody charge heterogeneity is proposed.
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Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Yelena Lyubarskaya, Damian Houde, James Woodard, David Murphy, Rohin Mhatre,