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The physical stability of a human growth hormone (hGH) formulation upon exposure to air/water interfaces (with vortex mixing) and to nonisothermal stress [determined by differential scanning calorimetry (DSC)] was investigated. The effect of these stresses on the formation of soluble and insoluble aggregates was studied. The aggregates were characterized(More)
Aggregation of peptide/protein drugs is of concern as it may lead to reduced bioactivity, immunogenic reactions, blockage of infusion pumps or unacceptable physical appearance. Aggregation of insulin and its prevention by carbohydrate excipients was investigated in this study. Aggregation was induced in solid-state by incubating with moisture at 37 degrees(More)
Several processing and shipping stresses were investigated for their effect on the physical stability of recombinant human growth hormone (rhGH). These included exposure to air/water interfaces, adsorption to hydrophobic surfaces, freeze-thaw cycles, and temperature. The interfacially and thermally denatured hormone was evaluated for the presence of(More)
Moisture-induced (2-10 microL added to 10 mg) aggregation of solid-state albumin and gamma-globulin was investigated by incubation at 37 degrees C for 24 h. The insoluble aggregates were centrifuged from a reconstituted solution, dissolved in a solution containing denaturant and reducing agent, and analysed by a Bio-Rad protein assay kit. Of the three(More)
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