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A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry.

Jonsson, AP (author)
Griffiths, WJ (author)
Bratt, P (author)
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Johansson, Ingegerd (author)
Umeå universitet,Kariologi
Strömberg, Nicklas (author)
Umeå universitet,Kariologi
Jörnvall, H (author)
Karolinska Institutet
Bergman, T (author)
Karolinska Institutet
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 (creator_code:org_t)
Wiley, 2000
2000
English.
In: FEBS Letters. - : Wiley. - 0014-5793 .- 1873-3468. ; 475:2, s. 131-4
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

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