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A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry
A P Jonsson1, W J Griffiths, P Bratt
1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
FEBS Letters
|June 20, 2000
Abstract:
Human acidic proline-rich salivary protein PRP-1 and its C-terminally truncated form PRP-3 were analyzed by electrospray tandem mass spectrometry. Post-translational modifications were detected and characterized. A pyroglutamic acid residue was demonstrated at the N-terminus, Ser-8 and Ser-22 were shown to be phosphorylated and an O-linked glucuronic acid conjugation was identified. The latter modification was located to Ser-17 and found to be present in approximately 40% of the polypeptides.