- Title
- Characterisation of tryptic peptides of phosphorylated tyrosine hydroxylase by high-pressure liquid chromatography electrospray ionisation mass spectrometry
- Creator
- Graham, Mark E.; Dickson, Phillip W.; Dunkley, Peter R.; von Nagy-Felsobuki, E. I.
- Relation
- Journal of Electron Spectroscopy and Related Phenomena Vol. 142, no. 3, p. 271-276
- Publisher
- Elsevier Science
- Resource Type
- journal article
- Date
- 2005
- Description
- Tyrosine hydroxylase (TH) is involved in the biosynthesis of catecholamines and is activated by phosphorylation. Phosphorylated TH was analysed using high-pressure liquid chromatogaphy 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 certainly of identification of phosphopeptides.
- Subject
- tyrosine hydroxylase; high-pressure liquid chromatography; electrospray; ionisation mass spectrometry; signal-to-noise ratio; selective detection; complex mixtures; identification; phosphopeptides; sites; sequence; mode
- Identifier
- uon:214
- Identifier
- http://hdl.handle.net/1959.13/25065
- Identifier
- ISSN:0368-2048
- Language
- eng
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