Format

Send to

Choose Destination
Nat Methods. 2013 Jan;10(1):54-6. doi: 10.1038/nmeth.2250. Epub 2012 Nov 18.

Digestion and depletion of abundant proteins improves proteomic coverage.

Author information

1
Department of Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA.

Abstract

Two major challenges in proteomics are the large number of proteins and their broad dynamic range in the cell. We exploited the abundance-dependent Michaelis-Menten kinetics of trypsin digestion to selectively digest and deplete abundant proteins with a method we call DigDeAPr. We validated the depletion mechanism with known yeast protein abundances, and we observed greater than threefold improvement in low-abundance human-protein identification and quantitation metrics. This methodology should be broadly applicable to many organisms, proteases and proteomic pipelines.

PMID:
23160281
PMCID:
PMC3531578
DOI:
10.1038/nmeth.2250
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center