The amino acid sequence of a glycosylated AL-chain from a patient with primary amyloidosis.
An amyloid fibril protein (Owe) related to primary amyloidosis was found to be a glycosylated complete immunoglobulin light chain (AL). The amino acid sequence revealed a protein composed of 214 residues and with a glycosylation site in position 20. The sequence established an AL V-region corresponding to a kappa 1b germline gene, but differs from that in 12 positions. Eight of them are in the FR-regions, positions 7, 13, 20, 42, 46, 60, 76 and 79. The J-segment is that of JkappaII.
Myran
Theresa
T
Biotechnology Centre of Oslo, University of Oslo, Norway.
Husby
Gunnar
G
Kyle
Robert A
RA
Sletten
Knut
K
D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000302:isolation & purification*; D000686:Amyloidosis / Q000378:metabolism* / Q000473:pathology; D005260:Female; D006031:Glycosylation; D006801:Humans; D007147:Immunoglobulin Light Chains / Q000737:chemistry*; D008875:Middle Aged; D008969:Molecular Sequence Data; D013154:Spleen / Q000737:chemistry / Q000473:pathology*
D000682:Amyloid; D007147:Immunoglobulin Light Chains