Studies of Protein Oxidation as a Product Quality Attribute on a Scale-Down Model for Cell Culture Process Development

References

1. 1.↵
   1. Li F.,
   2. Zhou J.,
   3. Yang X.,
   4. Tressel T.,
   5. Lee B.

   Current therapeutic antibody production and process optimization. BioProcessing J. 2005, 5 (4), 1–8.

   OpenUrlGoogle Scholar
2. 2.↵
   1. Goochee C. F.,
   2. Monica T.

   Environmental effects on protein glycosylation. Nature Biotechnol. 1990, 8 (5), 421–427.

   OpenUrlGoogle Scholar
3. 3.↵
   1. Konz J.,
   2. King J.,
   3. Cooney C.

   Effects of oxygen on recombinant protein expression. Biotechnology Progress. 1998, 14, 393–409.

   OpenUrlCrossRefPubMedWeb of ScienceGoogle Scholar
4. 4.↵
   1. Quiang L.,
   2. Harvey L.,
   3. McNeil B.

   Oxygen enrichment effects on protein oxidation, proteolytic activity and the energy status of submerged batch cultures of Aspergillus niger B1-D. Process Biochem. 2008, 43 (3), 238–243.

   OpenUrlGoogle Scholar
5. 5.↵
   1. Yang J.,
   2. Lu C.,
   3. Stansy B.,
   4. Henley J.,
   5. Guinto W.,
   6. Gonzalez C.,
   7. Gleason J.,
   8. Fung M.,
   9. Collopy B.,
   10. Benjamino M.,
   11. Gangi J.,
   12. Hanson M.,
   13. Ille E.

   Fed-batch bioreactor process scale-up from 3-L to 2,500-L scale for monoclonal antibody production from cell culture. Biotechnol. Bioeng. 2007, 98 (1), 141–154.

   OpenUrlPubMedGoogle Scholar
6. 6.↵
   1. Brorson K.,
   2. de Wit C.,
   3. Hamilton E.,
   4. Mustafa M.,
   5. Swann PG.,
   6. Kiss R.,
   7. Taticek R.,
   8. Polastri G.,
   9. Stein K. E.,
   10. Xu Y.

   Impact of cell culture process changes on endogenous retrovirus expression. Biotechnol. Bioeng. 2002, 80 (3), 257–267.

   OpenUrlPubMedGoogle Scholar
7. 7.↵
   1. Meuwly F.,
   2. Weber U.,
   3. Ziefler T.,
   4. Gervais A.,
   5. Mastrangeli R.,
   6. Crisci C.,
   7. Rossi M.,
   8. Bernard A.,
   9. von Stockar U.,
   10. Kadouri A.

   Conversion of CHO cell culture process from perfusion to fed-batch technology without altering product quality. J. Biotechnol. 2006, 123 (1), 106–116.

   OpenUrlPubMedGoogle Scholar
8. 8.↵
   Kondragunta et al. 2012.

   Google Scholar
9. 9.↵
   1. Naciri M.,
   2. Kuystermans D.,
   3. Al-Rubeai M.

   Monitoring pH and dissolved oxygen in mammalian cell culture using optical sensors. Cytotechnology 2008, 57 (3), 245–250.

   OpenUrlPubMedGoogle Scholar
10. 10.↵
    1. Eichhorn L. R.,
    2. Bartlett R. A.,
    3. Frey D. D.,
    4. Rao G.

    Noninvasive oxygen measurements and mass transfer considerations in tissue culture flasks. Biotechnol. Bioeng. 1996, 51 (4), 466–478.

    OpenUrlPubMedGoogle Scholar
11. 11.↵
    1. Dhir S.,
    2. Morrow K. J.,
    3. Rhinehart R. R.,
    4. Wesner T.

    Dynamic growth optimization of hybridoma growth in fed-batch bioreactor. Biotechnol. Bioeng. 2000, 67 (2), 197–205.

    OpenUrlPubMedGoogle Scholar
12. 12.↵
    1. Dasari V.,
    2. Rao K.,
    3. Ramu C.,
    4. Rao J.,
    5. Narasu M.,
    6. Rao A.

    Impact of dissolved oxygen concentration on some key parameters and production of rhG-CSF in batch fermentation. J. Ind. Microbiol. Biotechnol. 2008, 35 (9), 991–1000.

    OpenUrlPubMedGoogle Scholar
13. 13.↵
    1. Magi B.,
    2. Ettorre A.,
    3. Liveratori S.,
    4. Bini L.,
    5. Andreassi M.,
    6. Frosali S.,
    7. Neri P.,
    8. Pallini V.,
    9. Di Stefano A.

    Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: a cell biochemical and proteomic investigation. Cell Death Differ. 2004, 11 (8), 842–852.

    OpenUrlCrossRefPubMedGoogle Scholar
14. 14.↵
    1. Shacter E.

    Quantification and significance of protein oxidation in biological samples. Drug Metab. Rev. 2000, 32 (3–4), 307–326.

    OpenUrlCrossRefPubMedWeb of ScienceGoogle Scholar
15. 15.↵
    1. Soreghan B.,
    2. Yang F.,
    3. Thomas S.,
    4. Hsu J.,
    5. Yang A.

    High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharm. Res. 2003, 20 (11), 1713–1720.

    OpenUrlCrossRefPubMedWeb of ScienceGoogle Scholar
16. 16.↵
    1. Dalle-Donne I.,
    2. Rossi R.,
    3. Giustarini D.,
    4. Milzani A.,
    5. Colombo R.

    Protein carbonyl groups as biomarkers of oxidative stress. Clin. Chim. Acta 2002, 329 (1), 23–38.

    OpenUrlGoogle Scholar
17. 17.↵
    1. Buss I. H.,
    2. Chan T. P.,
    3. Sluis K. B.,
    4. Domigan N. M.,
    5. Winterbourn C. C.

    Protein carbonyl measurement by a sensitive ELISA method. Free Radic. Biol. Med. 1997, 23 (3), 361–366.

    OpenUrlCrossRefPubMedWeb of ScienceGoogle Scholar
18. 18.↵
    1. Vallejos J.,
    2. Brorson K.,
    3. Moreira A.,
    4. Rao G.

    Dissolved oxygen and pH profile evolution after cryovial thaw and repeated cell passaging in a T-75 flask. Biotechnol. Bioeng. 2006, 105 (6), 1040–1047.

    OpenUrlGoogle Scholar
19. 19.↵
    1. Riet K.

    Review of measuring methods and results in nonviscous gas-liquid mass transfer in stirred vessels. Ind. Eng. Chem. Process Des. Dev. 1979, 18 (3), 357–362.

    OpenUrlGoogle Scholar
20. 20.↵
    1. Kostov Y.,
    2. Harns P.,
    3. Randers-Eichhorn L.,
    4. Rao G.

    Low-cost microbioreactor for high-throughput bioprocessing. Biotechnol. Bioeng. 2001, 72 (3), 346–352.

    OpenUrlCrossRefPubMedWeb of ScienceGoogle Scholar
21. 21.↵
    1. Stadtman E. R.

    Role of oxidant species in aging. Current Medicinal Chemistry. 2004, 11, 1105–1112.

    OpenUrlCrossRefPubMedWeb of ScienceGoogle Scholar
22. 22.↵
    1. Saarinem M.,
    2. Murhammer D. W.

    The response of virally infected insect cells to dissolved oxygen concentration: recombinant protein production and oxidative damage. Biotechnol. Bioeng. 2003, 81 (1), 106–114.

    OpenUrlPubMedGoogle Scholar