Chapter title |
Identification of Carboxypeptidase Substrates by C-Terminal COFRADIC
|
---|---|
Chapter number | 9 |
Book title |
Protein Terminal Profiling
|
Published in |
Methods in molecular biology, March 2017
|
DOI | 10.1007/978-1-4939-6850-3_9 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6849-7, 978-1-4939-6850-3
|
Authors |
Tanco, Sebastian, Aviles, Francesc Xavier, Gevaert, Kris, Lorenzo, Julia, Van Damme, Petra, Sebastian Tanco, Francesc Xavier Aviles, Kris Gevaert, Julia Lorenzo, Petra Van Damme |
Editors |
Oliver Schilling |
Abstract |
We here present a detailed procedure for studying protein C-termini and their posttranslational modifications by C-terminal COFRADIC. In fact, this procedure can enrich for both C-terminal and N-terminal peptides through a combination of a strong cation exchange fractionation step at low pH, which removes the majority of nonterminal peptides in whole-proteome digests, while the actual COFRADIC step segregates C-terminal peptides from N-terminal peptides. When used in a differential mode, C-terminal COFRADIC allows for the identification of neo-C-termini generated by the action of proteases, which in turn leads to the identification of protease substrates. More specifically, this technology can be applied to determine the natural substrate repertoire of carboxypeptidases on a proteome-wide scale. |
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