Multiple oligosaccharide chains in the voltage-sensitive Na channel from Electrophorus electricus: Evidence for α-2,8-linked polysialic acid

William M. James, William S. Agnew

Research output: Contribution to journalArticle

Abstract

Carbohydrate substituents on the large peptide of the voltage-sensitive Na channel from Electrophorus electricus electroplax have been partially characterized by their sensitivity to endoglycosidases H and F, peptide:N-glycosidase F, Endo-N-acetylneuraminidase, and to neuraminidase. The results suggest the presence of at least two classes of oligosaccharides: neutral, high mannose or hybrid oligosaccharides, and acidic, complex oligosaccharides with a core-structure terminating in an unbranched homopolymer of sialosyl units in α-2,8 linkages (≫5 tandem sialic acids). Large decreases in apparent Mr produced by sialidase treatments suggest an extended carbohydrate structure that could inhibit protein-protein interaction. Polysialic acid was formerly proposed to be a unique constituent of neural cell adhesion molecules (N-CAMs) in vertebrates. However, ratios of sialic acid to galactose reported for mammalian brain and muscle Na channels suggest they may also carry this oligosaccharide.

Original languageEnglish (US)
Pages (from-to)817-826
Number of pages10
JournalBiochemical and Biophysical Research Communications
Volume148
Issue number2
DOIs
StatePublished - Oct 29 1987
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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