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LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification.

Nature methods (2014-11-25)
Pitter F Huesgen, Philipp F Lange, Lindsay D Rogers, Nestor Solis, Ulrich Eckhard, Oded Kleifeld, Theodoros Goulas, F Xavier Gomis-Rüth, Christopher M Overall
ABSTRACT

To improve proteome coverage and protein C-terminal identification, we characterized the Methanosarcina acetivorans thermophilic proteinase LysargiNase, which cleaves before lysine and arginine up to 55 °C. Unlike trypsin, LysargiNase-generated peptides had N-terminal lysine or arginine residues and fragmented with b ion-dominated spectra. This improved protein C terminal-peptide identification and several arginine-rich phosphosite assignments. Notably, cleavage also occurred at methylated or dimethylated lysine and arginine, facilitating detection of these epigenetic modifications.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
LysargiNase, suitable for peptide or protein digestion insolution or in gel
Sigma-Aldrich
Endoproteinase Arg-C from mouse submaxillary gland, suitable for protein sequencing, lyophilized powder

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