Abstract

Protein tyrosine sulfation (PTS) is an important post-translational modification that regulates a variety of physiological and pathological processes. However, PTS is unstable and lacks effective enrichment methods, which make it difficult to be detected in biological samples. In this study, we detected the tyrosine sulfation modification level of total proteins in developing zebrafish embryos by using high-resolution mass spectrometer, Orbitrap Exploris 480. A total of 26 proteins with tyrosine sulfation were detected, including membrane proteins, secreted proteins, cytoplasmic proteins and nucleoproteins. This study established a methodology in detecting protein tyrosine sulfation modification in embryonic zebrafish, which paved the way for evaluating the biological function of PTS.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call