Further Structural and Antigenic Studies of Light-chain Amyloid Proteins

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Abstract
The major subunit protein of amyloid fibrils (758) isolated from a patient with systemic amyloidosis and studied by N-terminal amino acid sequence analysis was found to be almost identical to the sequence of a VλIV Bence-Jones protein and a previously described AλIV amyloid protein. The two AλIV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-AλlV antiserum raised against one or the other of the two proteins. In addition, another new AλV amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the AλV subgroup (the AR protein). Finally, 20 primary or myeloma-associated amyloid proteins were characterized using antisera against the AA and several Ig light-chain-derived amyloid proteins.