Møyner K, Sletten K, Husby G, Natvig J B
Scand J Immunol. 1980;11(5):549-54. doi: 10.1111/j.1365-3083.1980.tb00023.x.
The amino acid sequence studies of a human amyloid fibril protein AA derived from a patient with Waldenström's macroglobulinaemia revealed 83 residues. This protein AA was larger than but otherwise very similar to other human AA proteins studied by complete sequencing. Two amino acids were found both in position 52 (Val/Ala) and in position 53 (Trp/Arg), strongly suggesting a polymorphism of AA proteins. Immunologic studies showed the antigenic determinant(s) reacting with antiprotein AA to be located between positions 25 and 76 of the third cyanogen bromide cleavage fragment of the protein.
对一名患有华氏巨球蛋白血症患者的人淀粉样原纤维蛋白AA进行的氨基酸序列研究显示有83个残基。该蛋白AA比通过完整测序研究的其他人AA蛋白更大,但在其他方面非常相似。在第52位(缬氨酸/丙氨酸)和第53位(色氨酸/精氨酸)均发现了两种氨基酸,这有力地表明了AA蛋白的多态性。免疫学研究表明,与抗蛋白AA反应的抗原决定簇位于该蛋白第三个溴化氰裂解片段的第25位和76位之间。