Journal article
Liquid Chromatography-Tandem Mass Spectrometry to Define Sortase Cleavage Products
Abstract
Sortase enzymes have specific endopeptidase activity, cleaving within a defined pentapeptide sequence at the C-terminal end of their protein substrates. Here, we describe how monitoring sortase cleavage activity can be achieved using peptide substrates. Peptide cleavage can be readily analyzed by liquid chromatography/tandem mass spectrometry (LC/MS/MS), which allows for the precise definition of cleavage sites. This technique could be used to …
Authors
Duong A; Koteva K; Sexton DL; Elliot MA
Journal
Methods in Molecular Biology, Vol. 1440, , pp. 99–108
Publisher
Springer Nature
Publication Date
2016
DOI
10.1007/978-1-4939-3676-2_8
ISSN
1064-3745