TCA precipitation and ethanol/HCl single-step purification evaluation: one-dimensional gel electrophoresis, bradford assays, spectrofluorometry and Raman spectroscopy data on HSA, Rnase, Lysozyme - Mascots and Skyline data on protein profiles from mouse liver, biofilm and soil samples

Publication date: Available online 5 February 2018
Source:Data in Brief
Author(s): Balkis Eddhif, Nadia Guignard, Yann Batonneau, Jonathan Clarhaut, Sébastien Papot, Claude Geffroy-Rodier, Pauline Poinot
The data presented here are related to the research paper entitled "Study of a Novel Agent for TCA Precipitated Proteins Washing - Comprehensive Insights into the Role of Ethanol/HCl on Molten Globule State by Multi-Spectroscopic Analyses" (Eddhif et al., 2017) [1]. The suitability of ethanol/HCl for the washing of TCA-precipitated proteins was first investigated on standard solution of HSA, cellulase, ribonuclease and lysozyme. Recoveries were assessed by one-dimensional gel electrophoresis, Bradford assays and UPLC-HRMS. The mechanistic that triggers protein conformational changes at each purification stage was then investigated by Raman spectroscopy and spectrofluorometry. Finally, the efficiency of the method was evaluated on three different complex samples (mouse liver, river biofilm, loamy soil surface). Proteins profiling was assessed by gel electrophoresis and by UPLC-HRMS.



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