Summary
Coupled high performance liquid chromatography/mass spectrometry (LC/MS) is utilized for the molecular weight determination of peptides from enzymatic digests of proteins. Methods designed to identify the individual peptides that contain sites of phosphorylation are described and demonstrated for the Lys C digest of the nicotinic acetylcholine receptor (AChR). The technique employs both the use of LC/MS and coupled LC/tandem mass spectrometry (LC/MS/MS) to screen for the neutral loss of phosphate from the peptides. The coupling of HPLC and mass spectrometry is accomplished through the use of an atmospheric pressure ionization source (API) and IonSpra® LC/MS interface on a triple quadrupole mass spectrometer.
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© 1991 Springer Basel AG
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Covey, T., Shushan, B., Bonner, R., Schröder, W., Hucho, F. (1991). LC/MS and LC/MS/MS Screening for the Sites of Post-Translational Modification in Proteins. In: Jörnvall, H., Höög, JO., Gustavsson, AM. (eds) Methods in Protein Sequence Analysis. Advances in Life Sciences. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-5678-2_25
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DOI: https://doi.org/10.1007/978-3-0348-5678-2_25
Publisher Name: Birkhäuser, Basel
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Online ISBN: 978-3-0348-5678-2
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