In:
Journal of Neurochemistry, Wiley, Vol. 54, No. 5 ( 1990-05), p. 1569-1575
Abstract:
Abstract: The mouse monoclonal antibody HNK‐1 and the human monoclonal IgM antibody present in patients with polyneuropathy both recognize carbohydrate epitope(s) on human myelin‐associated glycoprotein and P 0 . In the present study, the oligosaccharide structures that bear the antibody epitope(s) were investigated. The extracellular derivative of myelin‐associated glycoprotein (dMAG) was purified by immunoaffinity chromatography. P 0 was electroeluted from gel slices. Western blot analysis of whole glycoproteins demonstrated that the epitopes for HNK‐1 and the human monoclonal IgM antibody were different. The glycopeptides obtained by proteolysis of purified dMAG and P 0 were separated and characterized by affinity chromatography on concanavalin A‐Sepharose. Both dMAG and P 0 displayed heterogeneity in their oligosaccharide structures, i.e., they both contained mainly tri‐ and tetraantennary oligosaccharides (∼80%), although biantennary (10%) and high‐mannose and/or hybrid (10%) oligosaccharides were present. The human monoclonal IgM antibody epitope was present on all types of isolated oligosaccharide structures from either dMAG and P 0 . The HNK‐1 epitope was present on all types of oligosaccharide structures of dMAG, whereas it was present only on tri‐ and tetraantennary structures of P 0 .
Type of Medium:
Online Resource
ISSN:
0022-3042
,
1471-4159
DOI:
10.1111/jnc.1990.54.issue-5
DOI:
10.1111/j.1471-4159.1990.tb01206.x
Language:
English
Publisher:
Wiley
Publication Date:
1990
detail.hit.zdb_id:
2020528-4
SSG:
12
Bookmarklink