Isolation of the human myelin basic protein by immunoaffinity chromatography with a monoclonal antibody

Gábor J. Tigyi, Louisa Balázs, Éva Monostori, István Andó

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7 Citations (Scopus)

Abstract

Immunoaffinity chromatography has been developed for the isolation of the human myelin basic protein (MBP). The method is based on the use of a monoclonal antibody which was produced to bovine MBP, cross-reacting with human MBP. The protein isolated from acidic extracts of the brain proteins was shown to be native MBP by its immunochemical reactivity, by its ability to elicit experimental allergic encephalomyelitis and by its mol. wt (18,600 ± 400). It represented a single-band purity after hypersensitive silver staining. The MBP isolated by the method described represents a higher purity than that of the MBP purified by conventional multistep biochemical separation techniques.

Original languageEnglish
Pages (from-to)889-894
Number of pages6
JournalMolecular Immunology
Volume21
Issue number10
DOIs
Publication statusPublished - Oct 1984

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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