Structure and function of purified monoclonal antibody dimers induced by different stress conditions

Pharmaceutical Research

Volumn 29, Issue 8, 2012, Pages 2047-2059

  Paul, Rajsekhar ^a   Graff Meyer, Alexandra ^b   Stahlberg, Henning ^b   Lauer, Matthias E ^a   Rufer, Arne C ^a   Beck, Hermann ^a   Briguet, Alexandre ^a   Schnaible, Volker ^a   Buckel, Thomas ^a   Boeckle, Sabine ^a  

^a F HOFFMANN LA ROCHE LTD   (Switzerland)

^b UNIVERSITY OF BASEL   (Switzerland)

Author keywords

Antibody dimer Function; Monoclonal antibody; Protein aggregation; Structure

Indexed keywords

DIMER; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G1 MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY DIMER; UNCLASSIFIED DRUG;

ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; CHEMICAL ANALYSIS; CHEMICAL MODIFICATION; CHEMICAL STRUCTURE; CONCENTRATION RESPONSE; COVALENT BOND; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN CELL; HYDROPHOBICITY; LIGHT SCATTERING; LIGHT STRESS; MOLECULAR INTERACTION; MOLECULAR SIZE; MOLECULAR STABILITY; PH; PHYSICAL CHEMISTRY; PHYSICAL STRESS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PURIFICATION; STRESS; STRUCTURE ACTIVITY RELATION; SURFACE CHARGE; TRANSMISSION ELECTRON MICROSCOPY; ULTRAVIOLET RADIATION;

ANTIBODIES, MONOCLONAL; CHROMATOGRAPHY, GEL; HUMAN UMBILICAL VEIN ENDOTHELIAL CELLS; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN G; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; RECEPTORS, IGG; ULTRAVIOLET RAYS;

EID: 84864452495     PISSN: 07248741     EISSN: 1573904X     Source Type: Journal    
DOI: 10.1007/s11095-012-0732-6     Document Type: Article

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