Aggregation of Purified Protein Reference Materials Characterized by Asymmetric Flow Field Flow Fractionation

This is a file containing aggregation data for two proteins that were thermomechanically aggregated. The aggregated proteins were separated by asymmetric flow field flow fractionation and separated protein fractions were detected and quantified by UV spectrophotometry and multi-angle light scattering. The UV spectrophotometry was used to quantify the amount of residual monomer, which is reported herein. The multi-angle light scattering was fitted to a relevant model to calculate the molecular weight of the aggregated protein, also reported herein. The protein aggregation was characterized as a function of time and also the azide (preservative) concentration, which is indicated as being relevant to the aggregation process. The data contained here is plotted in a manuscript submitted to the Journal of Pharmaceutical Sciences and presented as part of that scientific record.