Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.

Article Details

Citation

Oxvig C, Haaning J, Hojrup P, Sottrup-Jensen L

Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum.

Biochem Mol Biol Int. 1994 May;33(2):329-36.

PubMed ID
7524900 [ View in PubMed
]
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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Bone marrow proteoglycanP13727Details