Summary
In this protocol, we describe an approach in which two-dimensional electrophoresis (2DE)-separated proteins are guanidinated in-gel prior to enzymatic cleavage. In contrast to previously described techniques, this procedure allows the extracted tryptic peptides to be N-terminally sulfonated without any further sample purification. The protocol was applied on a proteomic study of 2DE-separated proteins from Halorhodospira halophila, an extremophilic eubacterium with an unsequenced genome at the moment of analysis.
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Sergeant, K., Beeumen, J., Samyn, B. (2009). de Novo Sequence Analysis of N-Terminal Sulfonated Peptides After in-Gel Guanidination. In: Tyther, R., Sheehan, D. (eds) Two-Dimensional Electrophoresis Protocols. Methods in Molecular Biology, vol 519. Humana Press. https://doi.org/10.1007/978-1-59745-281-6_33
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DOI: https://doi.org/10.1007/978-1-59745-281-6_33
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