Complementary positional proteomics for screening substrates of endo- and exoproteases.
basic_science · Level V
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- Record sourced from PubMed, PMID 20526345.
- Also identified by DOI 10.1038/nmeth.1469.
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Abstract
We describe a positional proteomics approach to simultaneously analyze N- and C-terminal peptides and used it to screen for human protein substrates of granzyme B and carboxypeptidase A4 in human cell lysates. This approach allowed comprehensive proteome studies, and we report the identification of 965 database-annotated protein C termini, 334 neo-C termini resulting from granzyme B processing and 16 neo-C termini resulting from carboxypeptidase A4 processing.
Medical subject headings
- Carboxypeptidases A
- Granzymes
- Proteomics