Isolation of the human myelin basic protein by immunoaffinity chromatography with a monoclonal antibody |
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Authors: | Gábor J. Tigyi Louisa Balázs Éva Monostori István Andó |
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Affiliation: | 1. Institute of Genetics, Biological Research Centre, Hungarian Academy of Sciences, H-6701 Szeged, P.O. Box 521, Hungary;2. Institute of Pathology University Medical School, Pécs, Hungary |
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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. |
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Keywords: | MBP myelin basic protein EIA enzymelinked immunosorbent assay RIA radioimmunoassay SDS sodium dodecyl sulfate PBS phosphate-buffered physiological saline solution Ig immunoglobulin EAE experimental allergic encephalomyelitis HRPO horseradish peroxidase |
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