A human IgM M-protein in a patient with unknown bleeding disorder binds to beta-galactosyl and beta-glucosyl residues.
In 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.
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D005690:Galactose; D005947:Glucose; D006474:Hemorrhagic Disorders / Q000150:complications / Q000276:immunology*; D006801:Humans; D007075:Immunoglobulin M / Q000032:analysis* / Q000302:isolation & purification; D008875:Middle Aged; D010265:Paraproteinemias / Q000150:complications / Q000276:immunology*; D010314:Partial Thromboplastin Time
D007075:Immunoglobulin M; D005947:Glucose; D005690:Galactose