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Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum
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- Claus Oxvig
- J Haaning ,
- Peter Højrup, Institut for Biokemi og Molekylær Biologi, Denmark
- Lars Sottrup-Jensen, Denmark
From human pregnancy serum we have isolated the proform of eosinophil major basic protein (proMBP), which forms a complex with pregnancy-associated plasma protein-A (PAPP-A), PAPP-A/proMBP. It is shown that proMBP contains O-linked glycan bound to Ser-24, Thr-25 (fully substituted), and to Thr-23 and Thr-34 (partially substituted). N-linked glycan is bound to Asn-86 and O-linked glycosaminoglycan is bound to Ser-62 (both fully substituted). From the RP-HPLC elution profile and mass spectra of tryptic peptides it is found that proMBP is extremely heterogeneous with respect to glycosylation.
| Original language | English |
|---|---|
| Journal | Biochemistry and Molecular Biology International |
| Volume | 33 |
| Issue | 2 |
| Pages (from-to) | 329-336 |
| Number of pages | 8 |
| ISSN | 1039-9712 |
| Publication status | Published - May 1994 |
- Amino Acid Sequence, Blood Proteins, Carbohydrate Sequence, Carbohydrates, Chromatography, Gel, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Eosinophil Granule Proteins, Female, Glycosaminoglycans, Glycosylation, Humans, Molecular Sequence Data, Molecular Weight, Pregnancy, Pregnancy-Associated Plasma Protein-A, Protein Precursors, Ribonucleases
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