The covalent structure of amyloid-related serum protein SAA from two patients with inflammatory disease.
The complete covalent structure of an amyloid-related serum protein SAA from a patient (Jen.) with severe rheumatoid arthritis, is presented. The structure was elucidated by N-terminal analyses of the protein as well as on peptides derived from tryptic digestion and after cleaving the protein with BNPS-skatole. The characterization of tryptic peptide T-9 revealed a polymorphism similar to that seen in protein AA. Structural studies performed on another protein SAA, isolated from a patient (Mik.) with acute systemic lupus erythematosus, indicated that this protein is homologous to that from patient Jen. The formation and deposition of the protein AA-containing amyloid fibrils is discussed.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000682:Amyloid / Q000302:isolation & purification*; D001053:Apolipoproteins / Q000302:isolation & purification*; D001172:Arthritis, Rheumatoid / Q000097:blood*; D003488:Cyanogen Bromide; D006801:Humans; D008180:Lupus Erythematosus, Systemic / Q000097:blood*; D010446:Peptide Fragments / Q000032:analysis; D000685:Serum Amyloid A Protein / Q000302:isolation & purification*; D014357:Trypsin
D000596:Amino Acids; D000682:Amyloid; D001053:Apolipoproteins; D010446:Peptide Fragments; D000685:Serum Amyloid A Protein; C035165:apolipoprotein SAA; D014357:Trypsin; D003488:Cyanogen Bromide