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Amino Acid Sequences in Amyloid Proteins of χIII Immunoglobulin Light‐Chain Origin
Author(s) -
SLETTEN K.,
WESTERMARK P.,
PITKÄNEN P.,
THYRESSON N.,
OLSTAD O. K.
Publication year - 1983
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 - 10.1111/j.1365-3083.1983.tb00891.x
Subject(s) - immunoglobulin light chain , amyloidosis , bence jones protein , kappa , amyloid (mycology) , antibody , peptide sequence , amino acid , sequence (biology) , chemistry , al amyloidosis , amyloid fibril , biochemistry , microbiology and biotechnology , biology , medicine , immunology , pathology , gene , amyloid β , mathematics , inorganic chemistry , disease , geometry
The main amyloid fibril (AL) proteins extracted from the spleen of Patient So 124 with systemic amyloidosis and from a skin nodule of Patient KSA with localized amyloidosis were studied by partial amino acid sequence analysis and proved to be of χIII immunoglobulin light‐chain origin. The sequences were similar to that of Bence Jones protein Vand, which has been reported to have a unique χIII subset sequence. Thus, except for position 9 in protein AL(KSA), the amino acid sequences were identical to position 25 in AL(So 124) and in AL(KSA). The question is being raised whether this χIII subset might contain amyloidogenic sequences.