桥本氏血清M成分中抗甲状腺球蛋白抗体的克隆性受限。
Restricted clonality of antithyroglobulin antibodies in an M-component of Hashimoto's serum.
作者信息
Olivieri A, Salabè-Lotz H, Salabè G B
机构信息
Instituto di Medicina Sperimentale CNR, Roma, Italy.
出版信息
Thyroidology. 1990 Aug;2(2):65-71.
In serum of a 70 y. female with Hashimoto's thyroiditis we have identified an M-component IgG which is predominantly composed by a single class of antihuman thyroglobulin antibody. Our assumption is supported by Scatchard analysis and by the high concentration of lambda chains in serum and IgG fraction which are absorbed by h-thyroglobulin. Attempts to dissociate the monoclonal antibody treating the immunoprecipitate at acidic pH, were unsuccessful; only a few percent (3.7) of the antibodies could be released from immunoprecipitate and those were polyclonal. In order to explain the immunoprecipitating reaction of the monoclonal antibody, it is suggested that the antibody is reacting with a repetitive structure of the h-thyroglobulin molecule.
在一名患有桥本甲状腺炎的70岁女性血清中，我们鉴定出一种M成分IgG，其主要由单一类别的抗人甲状腺球蛋白抗体组成。我们的假设得到了Scatchard分析以及血清和IgG组分中高浓度的λ链（被人甲状腺球蛋白吸收）的支持。尝试在酸性pH条件下处理免疫沉淀物以解离单克隆抗体，但未成功；只有少数百分比（3.7%）的抗体能够从免疫沉淀物中释放出来，且这些是多克隆抗体。为了解释单克隆抗体的免疫沉淀反应，有人提出该抗体与人类甲状腺球蛋白分子的重复结构发生反应。
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