Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity

Journal of Pharmaceutical Sciences

Volumn 97, Issue 2, 2008, Pages 775-790

  Banks, Douglas D ^a   Gadgil, Himanshu S ^a   Pipes, Gary D ^b   Bondarenko, Pavel V ^b   Hobbs, Vipa ^b   Scavezze, Joanna L ^a   Kim, Jun ^b   Jiang, Xu Rong ^b   Mukku, Venkat ^b   Dillon, Thomas M ^b  

^a AMGEN INC   (United States)

^b AMGEN INC   (United States)

Author keywords

Mass spectrometry; Physical stability; Protein aggregation; Protein folding refolding; Protein formulation; Protein structure; Reduction; Spectroscopy; Stability

Indexed keywords

CYSTEINE; CYTOKINE; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G1; INTERLEUKIN 5; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MAB007; RECOMBINANT ANTIBODY; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DRUG FORMULATION; DRUG STABILITY; IMMUNOGLOBULIN STRUCTURE; LYMPHOCYTE PROLIFERATION; MOUSE; NONHUMAN; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN MODIFICATION; STRUCTURE ACTIVITY RELATION; T LYMPHOCYTE;

EID: 39749120684     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.21014     Document Type: Article

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