Lectin-enzyme assay as a method of estimation of immunoglobulins' glycosylation

A. M. Petrosyan, A. V. Britan

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

The mechanism of interaction of lectins with IgG molecules by the method of the lectin-enzyme assay has been described that allows to register a degree of human serum IgG molecules' glycosylation (mannosylation in case of lectin of Pisum sativum) in norm and at pathology. To detect an authentic difference in a glycosylation degree between control and pathological IgG, the wells of an ELISA plate were coated with an antibody in concentration of 1 μg/ml. Introducing α-D-mannose between the stages of incubation of immunoglobulin and lectin showed, that α-D-mannose inhibits the affinity of lectins for IgG. The preliminary incubation of lectin with IgG molecules stabilizes the activity of horseradish peroxidase, which labeled the lectins. Lectin-enzyme assay, in which Fab and Fc fragments of IgG were used, showed that lectin of Pisum sativum possesses a higher affinity for Fab regions. These findings and the glycosylation analysis of paraproteins and Bence-Jones proteins of multiple myeloma patients help to understand the details of interaction of immunoglobulins and lectins.

Original languageEnglish (US)
Pages (from-to)151-159
Number of pages9
JournalUkrain'skyi Biokhimichnyi Zhurnal
Volume78
Issue number4
StatePublished - Nov 27 2006

Keywords

  • Glycosylation
  • Immunoglobulin G
  • Lectin
  • Multiple myeloma

ASJC Scopus subject areas

  • Biochemistry

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