Stanworth D R, Henney C S
Immunology. 1967 Mar;12(3):267-74.
Human γG-globulin fractions rich in the dimeric (10S) form have been isolated from Cohn (Squibb) preparations, by repeated gel-filtration on Sephadex G-200. These fractions have been shown to fix complement and to precipitate rhemutaoid factor, despite the absence of larger aggregates (e.g. 20–40S) with which such activities are normally associated. In contrast, native human 7S γG-globulin preparations exhibited neither activity.
通过在Sephadex G - 200上反复进行凝胶过滤,已从科恩(施贵宝)制剂中分离出富含二聚体(10S)形式的人γG球蛋白组分。尽管不存在通常与这种活性相关的较大聚集体(例如20 - 40S),但这些组分已被证明能固定补体并沉淀类风湿因子。相比之下,天然的人7SγG球蛋白制剂均未表现出这种活性。