Effect of pH, temperature, and salt on the stability of Escherichia coli- and Chinese hamster ovary cell-derived IgG1 Fc

Biochemistry

Volumn 51, Issue 50, 2012, Pages 10056-10065

  Li, Cynthia H ^a   Narhi, Linda O ^a   Wen, Jie ^a   Dimitrova, Mariana ^b   Wen, Zai Qing ^a   Li, Jenny ^a   Pollastrini, Joseph ^a   Nguyen, Xichdao ^a   Tsuruda, Trace ^a   Jiang, Yijia ^a  

^a AMGEN INC   (United States)

^b MEDIMMUNE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE PEPTIDES; BIOPHYSICAL TECHNIQUES; CHINESE HAMSTER OVARY; CHINESE HAMSTER OVARY CELLS; E. COLI; EFFECT OF PH; EXTRACELLULAR DOMAINS; FUSION PROTEINS; GLYCOSYLATED; HIGH MOLECULAR WEIGHT; HIGH-ORDER STRUCTURE; HYDRODYNAMIC RADIUS; LONG-TERM STORAGE; MULTI-STEP; NEUTRAL PH; PHYSIOLOGICAL CONDITION; SALT CONCENTRATION; SECONDARY STRUCTURES; TERTIARY STRUCTURES; THERAPEUTIC PROTEIN; UNFOLDING PROCESS;

ESCHERICHIA COLI; MOLECULES; MONOCLONAL ANTIBODIES; PROTEINS;

PH EFFECTS;

HYBRID PROTEIN; IMMUNOGLOBULIN FC FRAGMENT; MONOCLONAL ANTIBODY; SODIUM CHLORIDE;

ANIMAL CELL; ARTICLE; BIOPHYSICS; CHO CELL; CONTROLLED STUDY; ESCHERICHIA COLI; GLYCOSYLATION; HEAT; HYDRODYNAMICS; MOLECULAR WEIGHT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN UNFOLDING; TEMPERATURE; THERMOSTABILITY;

ANIMALS; CHO CELLS; CRICETINAE; CRICETULUS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLYCOSYLATION; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; PROTEIN CONFORMATION; PROTEIN STABILITY; RECOMBINANT FUSION PROTEINS; SODIUM CHLORIDE; TEMPERATURE;

CRICETULUS GRISEUS; ESCHERICHIA COLI;

EID: 84871295525     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300702e     Document Type: Article

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