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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1996-12-10
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pubmed:abstractText |
High molecular weight precursors of insulin-like growth factor II (IGF-II) were isolated from Cohn fraction IV of human plasma by ultrafiltration, affinity chromatography and reversed-phase high-performance liquid chromatography. Molecular weight determination by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of two high molecular weight IGF-II preparations revealed heterogeneous glycosylation. A combination of enzymatic degradation and MALDI-MS were applied for further structural characterization of the glycosylated precursors of IGF-II. The first step was molecular weight determination of intact high molecular weight IGF-IIs prior to and after treatment with neuraminidase and O-glycosidase. This, together with a comparison of molecular weight information available from the cDNA, revealed that both high molecular weight IGF-II species contain an identical C-terminal extension of 20 residues but different degrees of glycosylation. Second, comparative Endo Glu-C digestion of the preparations prior to and after enzymatic release of carbohydrates and subsequent remeasurement of the molecular weight by MALDI-MS confirmed the primary structure of precursor IGF-II1-87. The O-linked carbohydrates were found to be associated with the C-terminal extension and the heterogeneity was identified as varied sialylated forms of one and two HexNAc-Hex groups.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor II,
http://linkedlifedata.com/resource/pubmed/chemical/Neuraminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1076-5174
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
31
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
893-900
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8799315-Amino Acid Sequence,
pubmed-meshheading:8799315-Glycoside Hydrolases,
pubmed-meshheading:8799315-Humans,
pubmed-meshheading:8799315-Hydrolysis,
pubmed-meshheading:8799315-Insulin-Like Growth Factor II,
pubmed-meshheading:8799315-Molecular Sequence Data,
pubmed-meshheading:8799315-Molecular Weight,
pubmed-meshheading:8799315-Neuraminidase,
pubmed-meshheading:8799315-Oligosaccharides,
pubmed-meshheading:8799315-Peptide Mapping,
pubmed-meshheading:8799315-Protein Precursors,
pubmed-meshheading:8799315-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
1996
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pubmed:articleTitle |
Characterization of O-glycosylated precursors of insulin-like growth factor II by matrix-assisted laser desorption/ionization mass spectrometry.
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pubmed:affiliation |
Division of Analytical Chemistry, University of Leiden, The Netherlands.
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pubmed:publicationType |
Journal Article
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