Gussakovskiĭ E E, Burshteĭn E A, Babaev T A
Biofizika. 1981 Mar-Apr;26(2):204-10.
Properties of tryptophane and tyrosine fluorescence of intact and iodinated thyroglobulin from normal human thyroid and nodular euthyroid goiter were studied. It has been shown that practically all (95%) tryptophane residues in "normal" thyroglobulin are in the inner regions of the globule. In "pathological" thyroglobulin in the regions inaccessible for water there are located only 68% of trypthophanyls. After iodination only in "pathological" thyroglobulin redistribution of tryptophan residues takes place on the surface and inside the globule. For bovine thyroglobulin shifts of tryptophane fluorescence spectra to the long wave region were observed, as well as a fall of the quantum yield at pH below 5 and above 11, which is in accord with acid and alkaline denaturation. A conformation transition was observed in the pH region 6--7 which is accompanied by a change in the efficiency of excitation energy transfer from tryptophan to iodoamino acids.
对来自正常人甲状腺和结节性甲状腺肿的完整及碘化甲状腺球蛋白的色氨酸和酪氨酸荧光特性进行了研究。结果表明，“正常”甲状腺球蛋白中几乎所有（95%）的色氨酸残基都位于球蛋白的内部区域。在“病理性”甲状腺球蛋白中，水难以到达的区域仅含有68%的色氨酸残基。碘化后，只有“病理性”甲状腺球蛋白中的色氨酸残基会在球蛋白表面和内部发生重新分布。对于牛甲状腺球蛋白，观察到色氨酸荧光光谱向长波区域移动，并且在pH低于5和高于11时量子产率下降，这与酸和碱变性相符。在pH值为6 - 7的区域观察到构象转变，同时伴随着从色氨酸到碘代氨基酸的激发能量转移效率的变化。
