Journal
ACS CHEMICAL BIOLOGY
Volume 6, Issue 10, Pages 1015-1020Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb200164h
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Funding
- National Institutes of Health [RR19355, RR22615]
- NIAID [AI068639]
- New York Speaker's Fund for Biomedical Research
- [T32CA062948]
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Many proteomic experiments require selective labeling of either N- or C-termini of proteins and recovery of terminal peptides. Although N-termini can be selectively labeled, selective labeling of protein C-termini has not been possible due to the difficulty in discriminating between the carboxyl group on the C-terminus versus that on aspartate and glutamate residues. Here we describe the first simple proteomic approach for positive selection of protein C-termini, Profiling Protein C-Termini by Enzymatic Labeling (ProC-TEL). ProC-TEL uses carboxypeptidase Y and other readily available reagents to selectively add an affinity tag to protein C-termini and to capture C-terminal peptides from complex cell lysates for mass spectrometry (MS) identification. Using ProC-TEL, we identify novel C-terminal processing and internal proteolytic cleavage events. These results indicate that ProC-TEL provides a straightforward approach for profiling C-terminal peptides and identifying protein processing in complex biological samples.
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