Shtrasburg S, Pras M, Langevitch P, Gal R
Am J Pathol. 1982 Feb;106(2):141-4.
AA-protein was identified by SDS-acrylamide electrophoresis in amyloid fibrils fixed in formalin after isolation from fresh-frozen tissues obtained from patients with familial Mediterranean fever (FMF) amyloidosis and idiopathic AA-amyloidosis and, following deparaffination, rehydration and homogenization of embedded formalin-fixed tissues of old autopsy cases of the hereditary amyloidosis of FMF and amyloidosis acquired in association with tuberculosis, bronchiectasis, and rheumatoid arthritis. That AA-protein is unaltered by formalin was firmly established by agar gel diffusion using specific rabbit anti-AA serum. By contrast, AL proteins could not be demonstrated either in formalin-fixed amyloid fibrils derived from fresh-frozen tissues of a patient with presumably AL-amyloidosis dominated by cardiomegaly and one with AL-kappa amyloidosis or in blocks of cases of familial neuropathic amyloidosis, multiple myeloma, and idiopathic amyloidosis with cardiopathy. AA-protein is not denatured by formalin and retains its typical electrophoretic, chromatographic, and immunologic characteristics even 30 years after fixation and paraffin-embedding.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳，在从家族性地中海热（FMF）淀粉样变性和特发性AA淀粉样变性患者获取的新鲜冷冻组织中分离出的经福尔马林固定的淀粉样原纤维中鉴定出AA蛋白；在FMF遗传性淀粉样变性以及与结核病、支气管扩张症和类风湿性关节炎相关的获得性淀粉样变性的旧尸检病例的福尔马林固定包埋组织进行脱蜡、复水和匀浆后，也鉴定出了AA蛋白。使用特异性兔抗AA血清通过琼脂凝胶扩散法确定福尔马林不会改变AA蛋白。相比之下，在来自一名以心脏肿大为主的疑似AL淀粉样变性患者和一名AL-κ淀粉样变性患者的新鲜冷冻组织的福尔马林固定淀粉样原纤维中，以及在家族性神经性淀粉样变性、多发性骨髓瘤和特发性心脏淀粉样变性病例的组织块中，均未检测到AL蛋白。AA蛋白不会被福尔马林变性，即使在固定和石蜡包埋30年后仍保留其典型的电泳、色谱和免疫特性。
