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Characterization of amyloidogenic immunoglobulin light chains directly from serum by on‐line immunoaffinity isolation
Author(s) -
Bergen H. Robert,
Abraham Roshini S.,
Johnson Kenneth L.,
Bradwell Arthur R.,
Naylor Stephen
Publication year - 2004
Publication title -
biomedical chromatography
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.4
H-Index - 65
eISSN - 1099-0801
pISSN - 0269-3879
DOI - 10.1002/bmc.323
Subject(s) - immunoglobulin light chain , chemistry , antibody , amyloid (mycology) , bence jones protein , dimer , amyloidosis , biochemistry , medicine , inorganic chemistry , organic chemistry , pathology , immunology , biology
Primary systemic amyloidosis (AL) is characterized by the overproduction of immunoglobulin light chain proteins by a monoclonal, terminally differentiated B‐lymphocyte or plasma cell clone. The free immunoglobulin light chains are deposited in an abnormal conformation as amyloid in a variety of organs in the body. The mechanism of amyloid formation is not well understood, but appears to be associated with some form of cleavage of the immunoglobulin light chain with subsequent aggregate formation. In an attempt to characterize the structure of amyloid‐forming light chain proteins we developed an on‐line immunoafnity purication and subsequent characterization of free κ and free λ immunoglobulin light chains by electrospray ionization mass spectrometry. The methodology is totally automated and requires 20 µL of serum. Mass spectral analysis of Bence Jones proteins under non‐denaturing conditions was also utilized to examine the tertiary and quaternary structure of light chain proteins and clearly shows covalent dimer formation of lambda type light chain. This type of on‐line assay may prove helpful in elucidating distinguishing features capable of discriminating AL from benign monoclonal gammopathies of undetermined signicance as well as diagnosing AL. Copyright © 2004 John Wiley & Sons, Ltd.

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