Ontology highlight
ABSTRACT:
SUBMITTER: Boersema PJ
PROVIDER: S-EPMC2667348 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Molecular & cellular proteomics : MCP 20081129 4
In this work, we explore the potential of the metalloendopeptidase Lys-N for MALDI-MS/MS proteomics applications. Initially we digested a HEK293 cellular lysate with Lys-N and, for comparison, in parallel with the protease Lys-C. The resulting peptides were separated by strong cation exchange to enrich and isolate peptides containing a single N-terminal lysine. MALDI-MS/MS analysis of these peptides yielded CID spectra with clear and often complete sequence ladders of b-ions. To test the applica ...[more]