The primary structure of the variable region of an immunoglobin IV light-chain amyloid-fibril protein (AL GIL).
The primary structure of the variable region of an amyloid-fibril protein GIL of immunoglobulin lambda-light-chain origin (AL) was determined. The AL protein obtained from the fibrils in the spleen of a 54-year-old man with primary systemic amyloidosis could be assigned to subgroup IV of the lambda variable-region sequence. About 50% of the protein was found to be truncated in the N-terminus and lacked the first six amino acid residues. The polypeptides consisted of about 146 amino acid residues and contained traces of carbohydrate. An acceptor site for N-glycosylation was found in positions 90-93, but no glycopeptide could be isolated. Comparison of the amino acid sequence of AL protein GIL with that of the only Bence-Jones protein of subgroup IV previously studied revealed a sequence homology of 89%. A similar comparison made with other AL proteins gave sequence homologies below 66%.
Fykse
E M
EM
Department of Biochemistry, University of Oslo, Blindern, Norway.
Sletten
K
K
Husby
G
G
Cornwell
G G
GG
D000595:Amino Acid Sequence; D000682:Amyloid; D006801:Humans; D007135:Immunoglobulin Variable Region; D007146:Immunoglobulin lambda-Chains; D008297:Male; D008875:Middle Aged; D008969:Molecular Sequence Data
D000682:Amyloid; D007135:Immunoglobulin Variable Region; D007146:Immunoglobulin lambda-Chains; C035222:amyloid protein AL