Abstract
Protein aggregation is typically thought of as a denaturation process that results in the formation of precipitate. However, native proteins may reversibly selfassociate to form discrete aggregates of dimer, trimer, and higher molecular weight forms. The rates of reversible aggregate association and dissociation vary dramatically from protein to protein and can lead to misconceptions regarding aggregate content if the incorrect assay is used to determine the extent of aggregation.
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Cromwell, M.E., Felten, C., Flores, H., Liu, J., Shire, S.J. (2006). Self-Association of Therapeutic Proteins. In: Misbehaving Proteins. Springer, New York, NY. https://doi.org/10.1007/978-0-387-36063-8_14
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DOI: https://doi.org/10.1007/978-0-387-36063-8_14
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