Separating full-length protein from aggregating proteolytic products using filter flow-through purification. Academic Article uri icon


  • Separation of full-length protein from proteolytic products is challenging, since the properties used to isolate the protein can also be present in proteolytic products. Many separation techniques risk non-specific protein adhesion and/or require a lot of time, enabling continued proteolysis and aggregation after lysis. We demonstrate that proteolytic products aggregate for two different proteins. As a result, full-length protein can be rapidly separated from these fragments by filter flow-through purification, resulting in a substantial protein purity enhancement. This rapid approach is likely to be useful for intrinsically disordered proteins, whose repetitive sequence composition and flexible nature can facilitate aggregation.

published proceedings

  • Anal Biochem

author list (cited authors)

  • Churion, K. A., Rogers, R. E., Bayless, K. J., & Bondos, S. E.

citation count

  • 0

complete list of authors

  • Churion, Kelly A||Rogers, Robert E||Bayless, Kayla J||Bondos, Sarah E

publication date

  • January 2016