A human IgM M-protein in a patient with unknown bleeding disorder binds to β-galactosyl and β-glucosyl residues

Susumu Kusunoki, Joseph E. Craft, Barbara Roach, John A. Hardin, Robert K. Yu

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

In a patient with an unknown bleeding disorder and an IgM λ 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 β-galactosyl or β-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 β-galactosyl and β-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.

Original languageEnglish (US)
Pages (from-to)226-232
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume255
Issue number2
DOIs
StatePublished - Jun 1987

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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