LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification.
Nat Methods
; 12(1): 55-8, 2015 Jan.
Article
em En
| MEDLINE
| ID: mdl-25419962
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.
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1
Base de dados:
MEDLINE
Assunto principal:
Proteômica
/
Metaloproteases
Tipo de estudo:
Diagnostic_studies
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article