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pubmed-article:3592674pubmed:abstractTextIn a patient with an unknown bleeding disorder and an IgM lambda paraproteinemia, we demonstrated by thin-layer chromatography immunostaining and enzyme-linked immunosorbent assay that this protein specifically bound to a number of glycolipids and glycoproteins which have terminal beta-galactosyl or beta-glucosyl residues. Binding to galactosylceramide or glucosylceramide was inhibited by both galactosylceramide and glucosylceramide. From these studies, it is apparent that the M-protein recognized both beta-galactosyl and beta-glucosyl residues. This M-protein was also shown to prolong the partial thromboplastin time of normal plasma. Thus, this case represents an example of anti-carbohydrate specificity of an IgM M-protein in association with a spontaneous bleeding disorder.lld:pubmed
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pubmed-article:3592674pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:3592674pubmed:articleTitleA human IgM M-protein in a patient with unknown bleeding disorder binds to beta-galactosyl and beta-glucosyl residues.lld:pubmed
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