Assessment of naturally occurring covalent and total dimer levels in human IgG1 and IgG2

Molecular Immunology

Volumn 58, Issue 1, 2014, Pages 108-115

  Yang, Jane ^a   Goetze, Andrew M ^a   Flynn, Gregory C ^a  

^a AMGEN INC   (United States)

Author keywords

Antibody structure; Disulfide formation; Disulfide isoforms; Oxidation reduction; Protein degradation

Indexed keywords

DIMER; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2;

ARTICLE; ARTIFACT; CIRCULATION; CONTROLLED STUDY; DILUTION; DIMERIZATION; HUMAN; HUMAN EXPERIMENT; IMMUNOGLOBULIN BLOOD LEVEL; NORMAL HUMAN; PRIORITY JOURNAL; SECRETORY CELL;

ANTIBODY STRUCTURE; DISULFIDE FORMATION; DISULFIDE ISOFORMS; DITHIOTHREITOL; DTT; EDTA; ETHYLENE DIAMINE TETRAACETIC ACID; GFB; GLUFIBRINOPEPTIDE B; HALF MOLECULE; HC; HEAVY CHAIN; HL; L-1-TOSYLAMIDO-2-PHENYLETHYL CHLOROMETHYL KETONE; LC; LC/MS; LIGHT CHAIN; LIQUID CHROMATOGRAPHY/MASS SPECTROMETRY; N-ETHYLMALEIMIDE; NEM; OXIDATION-REDUCTION; PROTEIN DEGRADATION; SDS-PAGE; SEC; SIZE-EXCLUSION CHROMATOGRAPHY; SODIUM DODECYL SULFATE-POLYACRYLAMIDE GEL ELECTROPHORESIS; TFA; TPCK; TRIFLUOROACETIC ACID; V(O); VOID VOLUME;

BLOOD DONORS; HUMANS; IMMUNOGLOBULIN G; PROTEIN ISOFORMS; PROTEIN MULTIMERIZATION;

EID: 84890047189     PISSN: 01615890     EISSN: 18729142     Source Type: Journal    
DOI: 10.1016/j.molimm.2013.11.011     Document Type: Article

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