[Intermolecular bonds of thyroglobulin].
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Biomedical subjects
Publications and source records attributed to T A Babaev.
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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.
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.