Sletten K, Marhaug G, Husby G
Hoppe Seylers Z Physiol Chem. 1983 Aug;364(8):1039-46. doi: 10.1515/bchm2.1983.364.2.1039.
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.
本文展示了一名患有严重类风湿性关节炎的患者(珍)血清中与淀粉样蛋白相关的血清淀粉样蛋白A(SAA)的完整共价结构。该结构通过对该蛋白进行N端分析以及对胰蛋白酶消化产生的肽段和用BNPS-粪臭素裂解该蛋白后得到的肽段进行分析得以阐明。对胰蛋白酶肽段T-9的表征揭示了一种与蛋白AA中所见类似的多态性。对从一名患有急性系统性红斑狼疮的患者(米克)分离出的另一种蛋白SAA进行的结构研究表明,该蛋白与患者珍的蛋白同源。文中还讨论了含蛋白AA的淀粉样纤维的形成和沉积。