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  • 1
    Language: English
    In: Pharmaceutical research, May 2013, Vol.30(5), pp.1380-99
    Description: To investigate antibody stability and formation of modified species under upstream processing conditions. The stability of 11 purified monoclonal human IgG1 and IgG4 antibodies, including an IgG1-based bispecific CrossMab, was compared in downscale mixing stress models. One of these molecules was further evaluated in realistic bioreactor stress models and in cell culture fermentations. Analytical techniques include size exclusion chromatography (SEC), turbidity measurements, cation exchange chromatography (cIEX), dynamic light scattering (DLS) and differential scanning calorimetry (DSC). Sensitivity in downscale stress models varies among antibodies and results in formation of high molecular weight (HMW) aggregates. Stability is increased in cell culture medium and in bioreactors. Media components stabilizing the proteins were identified. Extensive chemical modifications were detected both in stress models as well as during production of antibodies in cell culture fermentations. Protective compounds must be present in chemically defined fermentation media in order to stabilize antibodies against the formation of HMW aggregates. An increase in chemical modifications is detectable in bioreactor stress models and over the course of cell culture fermentations; this increase is dependent on the expression rate, pH, temperature and fermentation time. Consequently, product heterogeneity increases during upstream processing, and this compromises the product quality.
    Keywords: Antibodies, Monoclonal -- Chemistry ; Immunoglobulin G -- Chemistry
    ISSN: 07248741
    E-ISSN: 1573-904X
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  • 2
    Language: English
    In: Pharmaceutical Research, 2013, Vol.30(5), pp.1380-1399
    Keywords: aggregation ; antibodies ; deamidation ; fermentation ; stress models
    ISSN: 0724-8741
    E-ISSN: 1573-904X
    Source: Springer Science & Business Media B.V.
    Library Location Call Number Volume/Issue/Year Availability
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