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Bare silica as an alternative matrix for affinity purification/immobilization of His-tagged proteins 1 1 Introduction 1 2 Materials and methods 2 2.1 Construction of expression plasmids 2 2.2 Production and conventional purification of recombinant proteins 3 2.3 Binding and elution experiments 3 2.3.1 Adsorbent characteristics 3 2.3.2 Binding assays 3 2.3.3 Elution assays 3 2.4 One-step purification assays 3 2.5 Fluorescence spectroscopy and spectrophotometry analyses 4 2.6 Statistical analysis 4 3 Results and discussion 4 3.1 Binding and elution studies 4 3.1.1 Effect of pH, buffer composition and incubation time on His6-EGFP adsorption–desorption 4 3.1.2 Effect of adsorbent’s characteristics and equilibrium concentration on His6-EGFP binding 5 3.2 Small-scale batch purification of His6- and/or Car9-tagged proteins using bare silica particles 7 3.3 Scaled-up batch purification of His6-EGFP using bare silica particles 9 4 Conclusions 9 CRediT authorship contribution statement 10 Declaration of Competing Interest 10 Acknowledgements 10 Appendix A Supplementary data 10 References 10

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EN

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nonfiction