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Proteomic Profiling of Secreted Proteins from CHO Cells Using Surface‐Enhanced Laser Desorption Ionization Time‐of‐Flight Mass Spectrometry
Author(s) -
Kumar Niraj,
Maurya Priyanka,
Gammell Patrick,
Dowling Paul,
Clynes Martin,
Meleady Paula
Publication year - 2008
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp070244o
Subject(s) - chinese hamster ovary cell , mass spectrometry , proteome , chemistry , surface enhanced laser desorption/ionization , chromatography , proteomics , recombinant dna , cell culture , microbiology and biotechnology , protein mass spectrometry , biochemistry , biology , electrospray ionization , receptor , genetics , gene
Chinese hamster ovary (CHO) cells are the most commonly used host cell line for the production of recombinant biopharmaceuticals. These biopharmaceuticals are typically secreted from CHO cells and purified from harvested cell culture media. The purpose of this study was to investigate changes in the secreted proteome of CHO cells over the various stages of the growth cycle using Surface Enhanced Laser desorption ionization time‐of‐flight mass spectrometry (SELDI‐TOF MS). Conditioned media samples were collected each day over a 6 day growth period from CHO‐K1 cells grown in low serum (0.5% FBS) conditions in monolayer culture. Samples were profiled on a number of ProteinChip arrays with different chromatographic surfaces. From this study, 24 proteins were found to be differentially regulated at different phases of the growth cycle in CHO‐K1 cells, when profiled on two chromatographic surfaces, Q10 (anionic) and IMAC30 (metal affinity) ProteinChip arrays.