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

Gabor Tigyi, Louisa Balazs, Éva Monostori, István Andó

Research output: Contribution to journalArticle

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 (US)
Pages (from-to)889-894
Number of pages6
JournalMolecular Immunology
Volume21
Issue number10
DOIs
StatePublished - Jan 1 1984
Externally publishedYes

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Myelin Basic Protein
Chromatography
Monoclonal Antibodies
Silver Staining
Autoimmune Experimental Encephalomyelitis
Proteins
human MBP protein
Brain

All Science Journal Classification (ASJC) codes

  • Immunology
  • Molecular Biology

Cite this

Isolation of the human myelin basic protein by immunoaffinity chromatography with a monoclonal antibody. / Tigyi, Gabor; Balazs, Louisa; Monostori, Éva; Andó, István.

In: Molecular Immunology, Vol. 21, No. 10, 01.01.1984, p. 889-894.

Research output: Contribution to journalArticle

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