Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Karen Hurkmans"'
Autor:
Marisa Jones, Fengqiang Wang, Nisha Palackal, Lei Zhang, Emily Menesale, Nicole S Schonenbach, Thomas Waerner, Karen Hurkmans, Yiwei Zhao, Georgeen Gaza-Bulseco, Séverine Clavier, Satish Sharma, Trish Connolly, Pascal Valax, Suli Liu, Carmelata Chitikila
Publikováno v:
Biotechnology and Bioengineering. 118:2870-2885
Host cell proteins (HCPs) are process-related impurities that may copurify with biopharmaceutical drug products. Within this class of impurities there are some that are more problematic. These problematic HCPs can be considered high-risk and can incl
Autor:
Carmelata Chitikila, Thomas Waerner, Karen Hurkmans, Yiwei Zhao, Lei Zhang, Marisa Jones, Nisha Palackal, Suli Liu, Nicole S Schonenbach, Patricia Connolly, Séverine Clavier, Satish Sharma, Fengqiang Wang, Emily Menesale, Georgeen Gaza-Bulseco
Host cell proteins (HCPs) are process-related impurities that may co-purify with biopharmaceutical drug products. Within this class of impurities there are some that are more problematic. These problematic HCPs can be considered high-risk and can inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4baef39d0f1d0dbf7cce5c3a66893138
https://doi.org/10.22541/au.160266604.42218591/v1
https://doi.org/10.22541/au.160266604.42218591/v1
Publikováno v:
Analytical Chemistry. 82:5219-5226
One of the basic structural features of human IgG1 is the arrangement of the disulfide bond structure, 4 inter chain disulfide bonds in the hinge region and 12 intra chain disulfide bonds associated with twelve individual domains. Disulfide bond stru
Autor:
Sara Sinicropi-Yao, Chris Chumsae, Keith Hickman, Hongcheng Liu, Karen Hurkmans, Georgeen Gaza-Bulseco
Publikováno v:
Journal of Chromatography A. 1216:2382-2387
Glycosylation of the conserved asparagine residue in CH2 domains of IgG molecules is an important post-translational modification. The presence of oligosaccharides is critical for structure, stability and biological function of IgG antibodies. Effect
Publikováno v:
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences. 870(1)
Oxidation of methionine (Met) residues is one of the most common protein degradation pathways. Two Met residues, Met256 and Met432, of a recombinant fully human monoclonal IgG1 antibody have been shown to be susceptible to oxidation. Met256 and Met43