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Therapeutic Protein Products (therapeutic + protein_products)
Selected AbstractsPotential inaccurate quantitation and sizing of protein aggregates by size exclusion chromatography: Essential need to use orthogonal methods to assure the quality of therapeutic protein productsJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 5 2010John F. Carpenter First page of article [source] Immunogenicity of aggregates of recombinant human growth hormone in mouse modelsJOURNAL OF PHARMACEUTICAL SCIENCES, Issue 9 2009Amber Haynes Fradkin Abstract Aggregation of recombinant therapeutic protein products is a concern due to their potential to induce immune responses. We examined the immunogenicity of protein aggregates in commercial formulations of recombinant human growth hormone produced by freeze-thawing or agitation, two stresses commonly encountered during manufacturing, shipping and handling of therapeutic protein products. In addition, we subjected each preparation to high-pressure treatment to reduce the size and concentration of aggregates present in the samples. Aggregates existing in a commercial formulation, as well as aggregates induced by freeze-thawing and agitation stresses enhanced immunogenicity in one or more mouse models. The use of high-pressure treatment to reduce size and concentrations of aggregates within recombinant human growth hormone formulations reduced their overall immunogenicity in agreement with the "immunon" hypothesis. © 2009 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:3247,3264, 2009 [source] Overlooking subvisible particles in therapeutic protein products: Gaps that may compromise product quality,JOURNAL OF PHARMACEUTICAL SCIENCES, Issue 4 2009John F. Carpenter First page of article [source] Applications of mass spectrometry for the structural characterization of recombinant protein pharmaceuticalsMASS SPECTROMETRY REVIEWS, Issue 3 2007Catherine A. Srebalus Barnes Abstract Therapeutic proteins produced using recombinant DNA technologies are generally complex, heterogeneous, and subject to a variety of enzymatic or chemical modifications during expression, purification, and long-term storage. The use of mass spectrometry (MS) for the evaluation of recombinant protein sequence and structure provides detailed information regarding amino acid modifications and sequence alterations that have the potential to affect the safety and activity of therapeutic protein products. General MS approaches for the characterization of recombinant therapeutic protein products will be reviewed with particular attention given to the standard MS tools available in most biotechnology laboratories. A number of recent examples will be used to illustrate the utility of MS strategies for evaluation of recombinant protein heterogeneity resulting from post-translational modifications (PTMs), sequence variations generated from proteolysis or transcriptional/translational errors, and degradation products which are formed during processing or final product storage. Specific attention will be given to the MS characterization of monoclonal antibodies as a model system for large, glycosylated, recombinant proteins. Detailed examples highlighting the use of MS for the analysis of monoclonal antibody glycosylation, deamidation, and disulfide mapping will be used to illustrate the application of these techniques to a wide variety of heterogeneous therapeutic protein products. The potential use of MS to support the selection of cell line/clone selection and formulation development for therapeutic antibody products will also be discussed. © 2007 Wiley Periodicals, Inc., Mass Spec Rev [source] | ||||||||||