Development of LysargiNase, a mirror trypsin and its application in proteomics / 生物工程学报
Chinese Journal of Biotechnology
;
(12): 741-748, 2019.
Article
Dans Chinois
| WPRIM
| ID: wpr-771336
ABSTRACT
Proteomics is a fast-growing discipline that aims at systematic identification, quantification of proteins and their post-translational modifications in cells. Mass spectrometry-based shotgun proteomics technology is currently one of the mainstream methods for proteomics research. With this method, proteins need to be digested to peptides by site-specific proteases before they can be detected with mass spectrometry. Therefore, site-specific proteases played key roles in this process and so far, a variety of specific proteases have been developed and used in proteomics study. Particularly, the identification, characterization and development of proteases that cleave at the N-termini of corresponding amino acid residues, which are just mirrors to those of typical C-termini proteases, provide novel tools for proteomics analysis. In this review, we summarized the proprieties of LysargiNase, a most recently identified mirror trypsin, and its applications in proteomics research to promote its more widespread usage.
Texte intégral:
Disponible
Indice:
WPRIM (Pacifique occidental)
Sujet Principal:
Spectrométrie de masse
/
Trypsine
/
Chimie
/
Maturation post-traductionnelle des protéines
/
Protéomique
/
Metalloproteases
/
Métabolisme
langue:
Chinois
Texte intégral:
Chinese Journal of Biotechnology
Année:
2019
Type:
Article
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