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Biochem J. 1988 Apr 1;251(1):17-22.

Characterization of the binding epitope of a monoclonal antibody to sulphatide.

Author information

1
Department of Psychiatry and Neurochemistry, University of Gothenburg, Sweden.

Abstract

An IgG1 monoclonal antibody, Sulph I, reacting with sulphatide (3'-sulphogalactosylceramide), was produced by immunizing Balb/c mice with that glycolipid coated on Salmonella minnesota bacterial membrane. Radioimmunodetection of the binding of the monoclonal antibody to structurally related glycolipids adsorbed to microtitre plates or chromatographed on thin-layer plates was used to determine its binding epitope. The antibody showed similar binding avidity to three sulphated glycolipids: sulphatide, sulpholactosylceramide and seminolipid. Lysosulphatide did bind the antibody, but, compared with sulphatide, 30 times more antigen was needed for half-maximal binding. Bis(sulphogangliotriosyl)ceramide and bis-sulphogangliotetraosylceramide did not bind the antibody. These results suggest that terminal galactose-3-O-sulphate and part of the hydrophobic region of the glycolipid are recognized by the Sulph I antibody.

PMID:
2455508
PMCID:
PMC1148958
DOI:
10.1042/bj2510017
[Indexed for MEDLINE]
Free PMC Article

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