Further structural and antigenic studies of light-chain amyloid proteins.

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 V lambda IV Bence-Jones protein and a previously described A lambda IV amyloid protein. The two A lambda IV amyloid proteins showed strong antigenic cross-reaction, appearing as antigenic identity in double immunodiffusion tests using anti-A lambda IV antiserum raised against one or the other of the two proteins. In addition, another new A lambda V amyloid fibril protein (R.S.) showed strong amino acid sequence homology and antigenic identity in double immunodiffusions with the prototype of the A lambda V 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.

journal_name

Scand J Immunol

authors

Natvig JB,Westermark P,Sletten K,Husby G,Michaelsen T

doi

10.1111/j.1365-3083.1981.tb00187.x

subject

Has Abstract

pub_date

1981-07-01 00:00:00

pages

89-94

issue

1

eissn

0300-9475

issn

1365-3083

journal_volume

14

pub_type

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