Abstract
An immunochemical analysis was conducted to compare the C1 isomer of human myelin basic protein (MBP) with the newly described and less cationic, citrullinated isomer of MBP referres to as C8. Ten polyclonal antisera directed at multiple epitopes or restricted regions of MBP were used in radioimmunoassays to examine MBP-C1 and MBP-C8. Antisera reactive with MBP peptide 1–14 clearly distinguished MBP-C1 from MBP-C8. Antisera to human MBP peptides 10–19 and 90–170, but not to MBP peptide 69–89, showed modest differences between MBP-C1 and MBP-C8. The MBP-C8s from multiple sclerosis (MS) and non-MS brain reacted essentially the same. With murine monoclonal antibodies and enzyme-linked immunosorbent assay (ELISA), differences between MBP-C8 and other isomers were shown for anti-MBP 10–19 but not for anti-MBP 1–9 or anti-MBP 80–89. These findings imply differences in sequence or conformation in the structure of MBP-C8 compared to MBP-C1, most notably near the amino terminus.
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