Transient molten globules and metastable aggregates induced by brief exposure of a monoclonal IgG to Low pH

Journal of Pharmaceutical Sciences

Volumn 101, Issue 7, 2012, Pages 2327-2339

  Filipe, Vasco ^a,b   Kükrer, Başak ^a   Hawe, Andrea ^a   Jiskoot, Wim ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

^b UTRECHT UNIVERSITY   (Netherlands)

Author keywords

Kinetics; Protein aggregation; Protein folding refolding; Protein formulation; Protein structure

Indexed keywords

DIMER; IMMUNOGLOBULIN G ANTIBODY; MONOMER; NANOPARTICLE; OLIGOMER; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN;

ANALYTIC METHOD; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DYNAMIC LIGHT SCATTERING; FLUORESCENCE SPECTROSCOPY; GEL PERMEATION CHROMATOGRAPHY; LIGHT OBSCURATION; LIGHT SCATTERING; NANOPARTICLE TRACKING ANALYSIS; PARTICLE SIZE; PH; POLYMERIZATION; PROTEIN AGGREGATION; CHEMISTRY; GEL CHROMATOGRAPHY; HUMAN; KINETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; RADIATION SCATTERING; SPECTROFLUOROMETRY;

ANTIBODIES, MONOCLONAL; CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; HUMANS; HYDROGEN-ION CONCENTRATION; IMMUNOGLOBULIN G; KINETICS; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; SCATTERING, RADIATION; SPECTROMETRY, FLUORESCENCE;

EID: 84866265505     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1002/jps.23157     Document Type: Article

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