Benson M D, Skinner M, Lian J, Cohen A S
Arthritis Rheum. 1975 Jul-Aug;18(4):315-22. doi: 10.1002/art.1780180404.
A nonimmunoglobulin protein (A protein) has been isolated from amyloidotic tissue of secondary type. Antisera prepared to this protein identified a cross-reacting substance in the sera of patients with secondary amyloidosis. Sera from 70 persons with amyloidosis, 120 normal adults, 20 aged persons, and 97 patients with chronic diseases were tested for this substance. One hundred percent of secondary amyloid sera had amounts of amyloid serum component detectable by double diffusion in agar, whereas only 19 percent of primary amyloid sera were positive. Approximately 60 percent of rheumatoid sera as well as 60 per cent of sera from aged individuals were positive. Only 3 percent or normal blood donors had detectable amounts of this circulating substance. Isolation of the serum component by affinity chromatography and partial characterization have shown that it is an alpha-globulins with a molecular weight of 100,000-120,000, that it is not related antigenically to immunoglobulin or amyloid P-compoment, and that it has an amino acid analysis that is markedly different from tissue A protein. The possible participation of this substance in the genesis of amyloid is discussed.
已从继发性淀粉样变性组织中分离出一种非免疫球蛋白蛋白(A蛋白)。针对该蛋白制备的抗血清在继发性淀粉样变性患者血清中鉴定出一种交叉反应物质。对70例淀粉样变性患者、120名正常成年人、20名老年人以及97例慢性病患者的血清进行了该物质检测。100%的继发性淀粉样变性血清在琼脂双向扩散试验中可检测到淀粉样血清成分,而原发性淀粉样变性血清仅有19%呈阳性。约60%的类风湿血清以及60%的老年人血清呈阳性。仅3%的正常献血者血清中可检测到这种循环物质。通过亲和层析法分离血清成分并进行部分特性鉴定表明,它是一种分子量为100,000 - 120,000的α球蛋白,在抗原性上与免疫球蛋白或淀粉样P成分无关,且其氨基酸分析结果与组织A蛋白明显不同。本文讨论了该物质在淀粉样变性发生过程中可能的作用。