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Separating full-length protein from aggregating proteolytic products using filter flow-through purification | Academic Article individual record
abstract

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.

author list (cited authors)
Churion, K. A., Rogers, R. E., Bayless, K. J., & Bondos, S. E.
publication date
2016
publisher
Elsevier BV Publisher
published in
keywords
  • Intrinsically Disordered Protein
  • Proteolysis
  • Protein Purification
  • Filtration
  • Aggregation
  • Precipitation
citation count

0