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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-7-24
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
475
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-4
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10858503-Amino Acid Sequence,
pubmed-meshheading:10858503-Chromatography, High Pressure Liquid,
pubmed-meshheading:10858503-Glucuronic Acid,
pubmed-meshheading:10858503-Humans,
pubmed-meshheading:10858503-Mass Spectrometry,
pubmed-meshheading:10858503-Molecular Sequence Data,
pubmed-meshheading:10858503-Peptides,
pubmed-meshheading:10858503-Proline,
pubmed-meshheading:10858503-Proline-Rich Protein Domains,
pubmed-meshheading:10858503-Protein Processing, Post-Translational,
pubmed-meshheading:10858503-Serine,
pubmed-meshheading:10858503-Time Factors,
pubmed-meshheading:10858503-Trypsin
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pubmed:year |
2000
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pubmed:articleTitle |
A novel Ser O-glucuronidation in acidic proline-rich proteins identified by tandem mass spectrometry.
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pubmed:affiliation |
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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