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
в Zh
| WPRIM
| ID: wpr-771336
Ответственная библиотека:
WPRO
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.
Key words
Полный текст:
1
База данных:
WPRIM
Основная тема:
Mass Spectrometry
/
Trypsin
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Chemistry
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Protein Processing, Post-Translational
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Proteomics
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Metalloproteases
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Metabolism
Язык:
Zh
Журнал:
Chinese Journal of Biotechnology
Год:
2019
Тип:
Article