Large-scale identification of endogenous secretory peptides using electron transfer dissociation mass spectrometry.

ABSTRACT: Mass spectrometry-based unbiased analysis of the full complement of secretory peptides is expected to facilitate the identification of unknown biologically active peptides. However, tandem MS sequencing of endogenous peptides in their native form has proven difficult because they show size heterogeneity and contain multiple internal basic residues, the characteristics not found in peptide fragments produced by in vitro digestion. Endogenous peptides remain largely unexplored by electron transfer dissociation (ETD), despite its widespread use in bottom-up proteomics. We used ETD, in comparison to collision induced dissociation (CID), to identify endogenous peptides derived from secretory granules of a human endocrine cell line. For mass accuracy, both MS and tandem MS were analyzed on an Or

SUBMITTER: Sasaki K 

PROVIDER: S-EPMC3591662 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature