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 analyze the peptidase activity of any enzyme, and identify sites of cleavage within any peptide.

DOI: 10.1007/978-1-4939-3676-2_8

Cite this paper

@article{Duong2016LiquidCM, title={Liquid Chromatography-Tandem Mass Spectrometry to Define Sortase Cleavage Products.}, author={Andrew Duong and Kalinka P Koteva and Danielle L. Sexton and Marie A. Elliot}, journal={Methods in molecular biology}, year={2016}, volume={1440}, pages={99-108} }