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. 2017 Dec 5;22(12):2139. doi: 10.3390/molecules22122139

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© 2017 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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EGCG suppresses chaperone function of PfHsp70-1and PfHsp70-z. The independent chaperone functions of PfHsp70-1 (A) and PfHsp70-z (B) were investigated by monitoring the heat-induced aggregation of MDH in vitro at 48 °C, followed by quantitation of the pellet (P) and soluble (S) fractions, respectively. The assay was repeated in the presence of EGCG and/or nucleotides. The activity of PfHsp70-1 and PfHsp70-z in the presence of EGCG when compared to the activity of the respective protein either in nucleotide-free state or ADP bound state was statistically significant (p < 0.005). Statistical analysis was conducted using one way ANOVA. Standard deviations obtained from three replicate assays are shown.