Abstract

Three new IgG monoclonal antibodies are described which recognise sequential epitopes of the human myelin basic protein (MBP) molecule in amino acid sequences 36–50, 64–75 and 80–89. Two of the secreting hybridomas were prepared by immunisation of mice with synthetic peptides. This procedure appears to generate antibodies of similar affinities to those made using intact myelin basic protein as the immunogen. It has the advantage that antibodies to preselected regions of the molecule can be made at will and the problem of subsequent epitode localisation is simplified. It is possible with synthetic peptides to generate antibodies of specificities which it would be impossible to achieve by immunisation with intact myelin basic protein. The monoclonal antibodies described here should be useful tools in studies of myelin catabolism in vivo and in vitro. Of particular interest is our Clone 22, making an antibody which reacts equally well with intact human MBP and synthetic peptide sequence 80–89 in liquid phase assays. Antibodies of this rare specificity have been claimed to be able to react with the peptides of myelin basic protein found in the spinal fluid of patients with multiple sclerosis.

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