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Physical stability comparisons of IgG1-Fc variants: effects of N-glycosylation site occupancy and Asp/Gln residues at site Asn 297

The structural integrity and conformational stability of various IgG1-Fc proteins produced from the yeast Pichia pastoris with different glycosylation site occupancy (di-, mono-, and non- glycosylated) was determined. In addition, the physical stability profiles of three different forms of non-glyco...

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Détails bibliographiques
Publié dans:J Pharm Sci
Auteurs principaux: ALSENAIDY, MOHAMMAD A., OKBAZGHI, SOLOMON Z., KIM, JAE HYUN, JOSHI, SANGEETA B., MIDDAUGH, C. RUSSELL, TOLBERT, THOMAS J., VOLKIN, DAVID B.
Format: Artigo
Langue:Inglês
Publié: 2014
Sujets:
Accès en ligne:https://ncbi.nlm.nih.gov/pmc/articles/PMC4512762/
https://ncbi.nlm.nih.gov/pubmed/24740840
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/jps.23975
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