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Preparation and Properties of Antibodies to G D3 and G M1 Gangliosides
Author(s) -
Kundu Samar K.,
Marcus Donald M.,
Ven Rüdiger W.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb04638.x
Subject(s) - ganglioside , chemistry , antibody , sialic acid , periodate , biochemistry , bovine serum albumin , neuraminidase , antiserum , residue (chemistry) , glycolipid , affinity chromatography , biology , enzyme , immunology
Gangliosides G D3 and G M1 were coupled to proteins by their car‐boxyl groups and antisera were raised against the complexes. Anti‐ganglioside antibodies were isolated by affinity chromatography on ganglioside‐amino‐propyl silica gel columns and the specificity of the antibodies was determined by a quantitative microcomplement fixation assay. Antibodies to G D3 were highly specific and did not crossreact with G M3 , lactosyl ceramide, or other glycolipids. Purified antibodies to G M1 , in contrast, crossreacted with asialo‐G M1 , G D1b and to a lesser extent, G M2 and asialo‐G M2 . A derivative of G M1 , containing a C‐7 sialic acid residue produced by periodate oxidation, reacted with the anti‐G M1 antibodies almost as readily as with G M1 . The specificities of anti‐G M1 antibodies elicited by the covalent ganglioside‐protein complexes were similar to those produced by immunization with noncovalent complexes of G M1 and methylated bovine serum albumin. The ganglioside‐protein complexes described here should be useful for preparing antibodies to polysialo‐gangliosides that contain neuraminidase‐sensitive linkages.