Dimers and multimers of monoclonal IgG1 exhibit higher in vitro binding affinities to Fcγ receptors

mAbs

Volumn 1, Issue 5, 2009, Pages 491-504

  Luo, Yin ^a   Lu, Zhaojiang ^a   Raso, Stephen W ^a   Entrican, Clifford ^a   Tangarone, Bruce ^a  

^a PFIZER INC   (United States)

Author keywords

Fc receptors; Fc RIIA; Fc RIIIB; IgG; Immune complex; In vitro binding; Protein aggregation; Surface plasmon resonance

Indexed keywords

CD16 ANTIGEN; DIMER; FC RECEPTOR; FC RECEPTOR IIA; FC RECEPTOR IIB; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1; MONOCLONAL ANTIBODY 2; POLYMER; UNCLASSIFIED DRUG; IMMUNOGLOBULIN G;

ANIMAL CELL; ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CHO CELL; CONTROLLED STUDY; DIMERIZATION; DISSOCIATION; NONHUMAN; RECEPTOR BINDING; SURFACE PLASMON RESONANCE; ANIMAL; ANTIBODY AFFINITY; ANTIGEN ANTIBODY COMPLEX; BINDING SITE; CHEMISTRY; CRICETULUS; GENETIC PROCEDURES; HAMSTER; HUMAN; KINETICS; METABOLISM; PROTEIN BINDING; PROTEIN MULTIMERIZATION;

ANIMALS; ANTIBODIES, MONOCLONAL; ANTIBODY AFFINITY; ANTIGEN-ANTIBODY COMPLEX; BINDING SITES; BIOSENSING TECHNIQUES; CHO CELLS; CRICETINAE; CRICETULUS; DIMERIZATION; HUMANS; IMMUNOGLOBULIN G; KINETICS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; RECEPTORS, IGG; SURFACE PLASMON RESONANCE;

EID: 77953669816     PISSN: 19420862     EISSN: None     Source Type: Journal    
DOI: 10.4161/mabs.1.5.9631     Document Type: Article

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