title: Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.
abstract: 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.
authors.affiliation: Department of Molecular Biology, University of Aarhus, Denmark.
authors.forename: C
authors.initials: C
authors.lastname: Oxvig
authors.forename: J
authors.initials: J
authors.lastname: Haaning
authors.forename: P
authors.initials: P
authors.lastname: Højrup
authors.forename: L
authors.initials: L
authors.lastname: Sottrup-Jensen
mesh_terms: D000595:Amino Acid Sequence; D001798:Blood Proteins / Q000737:chemistry* / Q000378:metabolism; D002240:Carbohydrate Sequence; D002241:Carbohydrates / Q000032:analysis*; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D047091:Eosinophil Granule Proteins; D005260:Female; D006025:Glycosaminoglycans / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011247:Pregnancy / Q000097:blood*; D011266:Pregnancy-Associated Plasma Protein-A / Q000378:metabolism*; D011498:Protein Precursors / Q000097:blood / Q000737:chemistry* / Q000378:metabolism; D012260:Ribonucleases
chemical_list: D001798:Blood Proteins; D002241:Carbohydrates; D047091:Eosinophil Granule Proteins; D006025:Glycosaminoglycans; D011498:Protein Precursors; D012260:Ribonucleases; D011266:Pregnancy-Associated Plasma Protein-A