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A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry.
Umeå University, Faculty of Medicine, Odontology, Cariology.
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2000 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 475, no 2, 131-4 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2000. Vol. 475, no 2, 131-4 p.
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URN: urn:nbn:se:umu:diva-8916PubMedID: 10858503OAI: oai:DiVA.org:umu-8916DiVA: diva2:148587
Available from: 2008-02-21 Created: 2008-02-21 Last updated: 2017-12-14Bibliographically approved

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