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Constant Region of a κ III Immunoglobulin Light Chain as a Major AL‐Amyloid Protein
Author(s) -
J P Engvig,
Karen Ege Olsen,
Randi Elin Gislefoss,
Knut Sletten,
Ola Wahlström,
Per Westermark
Publication year - 1998
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.1998.00352.x
Subject(s) - immunoglobulin light chain , antibody , amyloid (mycology) , constant (computer programming) , chemistry , immunoglobulin g , microbiology and biotechnology , biology , immunology , computer science , inorganic chemistry , programming language
AL‐amyloidoses are generally described as a group of disorders in which N‐terminal fragments of monoclonal immunoglobulin light chains are transferred into amyloid fibrils. We have, by amino acid sequence analyses and immunological methods, characterized the Bence‐Jones protein and the corresponding AL protein as a κ III immunoglobulin light chain from material of a patient with systemic AL‐amyloidosis presenting as a local inguinal tumour. The two proteins showed some unique features. The major part of the AL amyloid fibril protein consisted of C‐terminal fragments of the Bence‐Jones protein. Furthermore, both the Bence‐Jones protein and the AL protein were glycosylated, with possibly a glycosylation in the constant part of the light chain.