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- W4309660147 abstract "A critical step in the functional characterization of proteases is the identification of physiologically relevant substrates, which often starts with a collection of candidate proteins. To test these candidates and identify specific processing sites, in vitro cleavage assays are typically used, followed by polyacrylamide gel electrophoresis (SDS-PAGE) to separate and visualize the cleavage products. For the identification of cleavage sites, the sequences at the N- or C-terminal ends of the cleavage products need to be identified, which is the most challenging step in this procedure. Here, we describe a method for the reliable identification of the N-termini of polypeptides after separation by SDS-PAGE. The procedure relies on in-gel labeling of the N-terminal-free amino group by reductive dimethylation, followed by tryptic digestion and analysis of resulting peptides by mass spectrometry. N-terminal peptides are readily identified by the 28 Da mass dimethyl tag linked to their first amino acid." @default.
- W4309660147 created "2022-11-29" @default.
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- W4309660147 date "2022-11-23" @default.
- W4309660147 modified "2023-09-23" @default.
- W4309660147 title "Improved Identification of Protease Cleavage Sites by In-gel Reductive Dimethylation" @default.
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- W4309660147 doi "https://doi.org/10.1007/978-1-0716-2784-6_24" @default.
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