Effect of protein structure on deamidation rate in the Fc fragment of an IgG1 monoclonal antibody

Protein Science

Volumn 18, Issue 8, 2009, Pages 1573-1584

  Sinha, Sandipan ^a,c   Zhang, Lei ^a   Duan, Shaofeng ^a   Williams, Todd D ^a   Vlasak, Josef ^b   Ionescu, Roxana ^b   Topp, Elizabeth M ^a,d  

^a UNIVERSITY OF KANSAS   (United States)

^b MERCK RESEARCH LABORATORIES   (United States)

^c PFIZER GLOBAL RESEARCH AND DEVELOPMENT   (United States)

^d PURDUE UNIVERSITY   (United States)

Author keywords

Deamidation; IgG1; Monoclonal antibody; Protein stability; Secondary structure

Indexed keywords

ASPARAGINE; ASPARTIC ACID; HUMAN MONOCLONAL ANTIBODY; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1 ANTIBODY; ISOASPARTIC ACID; PAPAIN; SUCCINIMIDE; SYNTHETIC PEPTIDE; TRASTUZUMAB;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DEAMINATION; ELECTROSPRAY MASS SPECTROMETRY; FRAGMENTATION REACTION; HALF LIFE TIME; HUMAN; ISOMERIZATION; KINETICS; LIQUID CHROMATOGRAPHY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; TANDEM MASS SPECTROMETRY;

AMIDES; AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; ASPARAGINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; HUMANS; IMMUNOGLOBULIN FC FRAGMENTS; IMMUNOGLOBULIN G; KINETICS; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; TANDEM MASS SPECTROMETRY;

EID: 67749109890     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.173     Document Type: Article

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