| Popis: |
The recombinant ppTvCP4 (ppTvCP4r) protein, a specific inhibitor of the proteolytic activity and virulence properties of Trichomonas vaginalis, depending on cathepsin L-like cysteine proteinases (CPs) (http:dx.doi.org/ 10.1016/j.biocel.2014.12.001 [1], http:dx.doi.org/ 10.1016/j.micinf.2013.09.002 [2], http:dx.doi.org/ 10.1155/2015/946787 [3]) was stable in the elution buffer up to two months at 4 °C. However, it was prone to aggregate in PBS (functional assay buffer) [1]. Therefore, before functional assays, the aggregation kinetic of refolded ppTvCP4r was determined after the exchange to PBS. Samples of purified and refolded ppTvCP4r (0.15 mg/ml) in PBS were incubated for 0–24 h at 4 and 25 °C, spun down, measured the protein concentration in the supernatant and checked for the presence of aggregated protein in the pellet. The concentration of protein progressively decreased in the supernatant through time at both temperatures as the protein aggregated. Data in this article are related to the research paper [1]. Keywords: PpTvCP4r, Buffer exchange, Protein aggregation, Trichomonas vaginalis |
