Abstract
Low concentrations of antibrain antibody can be detected in cerebrospinal fluid (CSF) from most patients with multiple sclerosis and a few patients with other neurologic diseases.
The CSF antibody specificities, detected by the sensitive enzyme-linked immunosorbent assay (ELISA), have been utilized to characterize brain ‘target’ antigens in chromatofocused fractions of brain extracts. In order to compare the antigenic composition of extracts and fractions which are recognized by antibrain antibodies, without wasting limited quantities of CSF or serum, a versatile method for specific absorption of antibody on the ELISA plates was developed. Polyvinyl chloride (PVC) plates, pretreated with glutaric dialdehyde (to bind antigens irreversibly), were coated with the adsorbing antigen and the antibody mixture was incubated to remove specific reactivity before transfer to a second PVC plate coated with the test antigen. Under optimal conditions this method could remove specifically more than 80% of anti-myelin basic protein (MBP) reactivity with a single absorption. By comparing reactive and preabsorbed rabbit anti-MBP antiserum, both native MBP and MBP fragments or complexes could be detected in chromatofocused fractions of MS brain extracts.
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Van Rompaey, F., Nijst, D., Raus, J., Vandenbark, A.A. (1984). Antibrain antibody adsorption on microtitre plates. In: Gonsette, R.E., Delmotte, P. (eds) Immunological and Clinical Aspects of Multiple Sclerosis. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-6352-1_92
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DOI: https://doi.org/10.1007/978-94-011-6352-1_92
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-011-6354-5
Online ISBN: 978-94-011-6352-1
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