Epitope Mapping of TTR (Prealbumin) and TTR(Met30) with Monoclonal Antibodies
Familial Amyloidotic Polyneuropathy, type I, is an inherited autossomal dominant disease in which an abnormal TTR with a methionine for valine substitution at position 30 (TTR(Met30)) was demonstrated1,2, both in the amyloid fibrils and in patients serum. However, it does not differ from normal TTR in most physicochemical properties studied3, including the electrophoretic mobility and ligand affinities, thus making detection and purification difficult. A significative improvement in this situation would be achieved if a monoclonal antibody (mab) selective for the abnormal protein could be developed. A likely requirement for such a mab is that it recognizes an epitope that includes the mutation point, so the mabs we have so far obtained were tested against peptides derived from TTR by tryptic digestion and CNBr cleavage, in an attempt to define those epitopes.
KeywordsAmyloid Fibril Tryptic Digestion Myeloma Cell Line Ligand Affinity Karolinska Hospital
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