Abramov A A, Gussakovskiĭ E E, Babaev T A
Vopr Med Khim. 1983 Mar-Apr;29(2):26-9.
Intact and iodine-treated thyroglobulin from normal thyroid gland and from nodular euthyroid goiter were studied by means of circular dichroism to detect differences in the protein secondary structure. Contents of alpha- and beta-structures in thyroglobulins were differentiated only by several per cents but artificial iodination of the protein increased markedly the difference between thyroglobulins of various origin. Extrapolation of the data to "zero" content of iodine-containing amino acids demonstrated that the initial steps of thyroglobulin synthesis occurring before iodination "in vitro", appears to be also responsible for alterations in the protein secondary structure.
利用圆二色性对来自正常甲状腺和结节性甲状腺肿的完整及经碘处理的甲状腺球蛋白进行了研究，以检测蛋白质二级结构的差异。甲状腺球蛋白中α-结构和β-结构的含量仅相差几个百分点，但蛋白质的人工碘化显著增加了不同来源甲状腺球蛋白之间的差异。将数据外推至含碘氨基酸“零”含量表明，甲状腺球蛋白合成在“体外”碘化之前发生的初始步骤，似乎也导致了蛋白质二级结构的改变。
