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- W4383216766 abstract "The PARP1 (Poly (ADP-ribose) polymerase 1) enzyme is essential for single and double-strand break repair in humans. Alterations affecting PARP1 activity have severe consequences for human health and are associated with pathologies like cancer, and metabolic and neurodegenerative disorders. Here, we have developed a fast and easy procedure for the expression and purification of PARP1. Biologically active protein was purified to an apparent purity >95%, with only two purification steps. A thermostability analysis revealed that PARP1 possessed improved stability in 50 mM Tris-HCl pH 8.0 (Tm = 44.2 ± 0.3 °C), thus this buffer was used throughout the whole purification procedure. The protein was shown to bind to DNA and has no inhibitor molecules bound to the active site. Finally, the yield of the purified PARP1 protein is sufficient for both biochemical, biophysical and structural analysis. The new protocol is more effective and produces similar protein quantities in less time." @default.
- W4383216766 created "2023-07-06" @default.
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- W4383216766 date "2023-11-01" @default.
- W4383216766 modified "2023-09-27" @default.
- W4383216766 title "Advances in the expression and purification of human PARP1: A user-friendly protocol" @default.
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- W4383216766 doi "https://doi.org/10.1016/j.pep.2023.106336" @default.
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