![]() hirsuta and identified using mass spectrometry, which confirms the applicability of this protocol for liverworts proteomics. Furthermore, we randomly selected spots from the 2-DE gel of D. hirsuta and other two liverworts, i.e., Marchantia paleacea and Plagiochasma appendiculatum. The modifications provided us better results in terms of protein yield, resolution, spot numbers, and intensities for 2-DE gels of D. Furthermore, we performed modifications during protein washing, re-solubilization in rehydration buffer and isoelectric focusing (IEF). Among these methods, 50 mM Tris–HCl (pH 7.5) extraction, followed by 20% TCA–acetone precipitation, appeared to be more suitable for 2-DE. We compared three different protein extraction methods, i.e.,1.5 M Tris–HCl (pH 8.8), 50 mM Tris–HCl (pH 7.5), and polyvinylpolypyrrolidone (PVPP) extraction, followed by three precipitation methods, i.e., 80% ethanol, 80% acetone, and 20% tricholoroacetic acid (TCA)–acetone, in a liverwort Dumortiera hirsuta. Herein, we highlight the comparison and optimization of an effective protein extraction and precipitation protocol for two-dimensional gel electrophoresis (2-DE) of liverworts. Proteomics is a state-of-the-art technique that can capture snapshots of events occurring at the protein level in many organisms. ![]() Liverworts possess historical adaptive strategies for abiotic stresses because they were the first plants that shifted from water to land. ![]()
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