Characterisation of tryptic peptides of phosphorylated tyrosine hydroxylase by high-pressure liquid chromatography electrospray ionisation mass spectrometry
Journal of Electron Spectroscopy and Related Phenomena, ISSN: 0368-2048, Vol: 142, Issue: 3, Page: 271-276
2005
- 3Citations
- 4Captures
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Article Description
Tyrosine hydroxylase (TH) is involved in the biosynthesis of catecholamines and is activated by phosphorylation. Phosphorylated TH was analysed using high-pressure liquid chromatography combined with electrospray mass spectrometry (HPLC ESI-MS). Two mass scanning methods were used to detect tryptic cleavage products of TH. In the positive electrospray ionisation mode (ESI+), the peptides that contain the phosphorylation sites of TH were identified. In the alternative method, a phosphopeptide was detected in the negative electrospray ionisation mode (ESI−) using single ion monitoring in combination with a sequential ESI+ switching experiment. A raised baseline interfered with detection of hydrophilic peptides in ESI−, with the signal-to-noise ratio indicating that the method was operating near the limit of detection for a conventional electrospray source. The switching method improved the certainty of identification of phosphopeptides.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0368204804003664; http://dx.doi.org/10.1016/j.elspec.2004.09.008; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=13244283287&origin=inward; https://linkinghub.elsevier.com/retrieve/pii/S0368204804003664; https://api.elsevier.com/content/article/PII:S0368204804003664?httpAccept=text/xml; https://api.elsevier.com/content/article/PII:S0368204804003664?httpAccept=text/plain; https://dx.doi.org/10.1016/j.elspec.2004.09.008
Elsevier BV
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