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Thyroglobulin structure-function: the effect of iodination on the structure of human thyroglobulin.

Abstract：

:Thyroglobulin of very low iodine content has been prepared from a single non-toxic human goitre. The initial iodine content of the protein (0.038%) has been increased to levels of 0.16% and 0.85% by in vitro treatment with thyroid peroxidase and the resulting proteins studied with respect to their intrinsic fluorescence, circular dichroism spectra and binding of the hydrophobic probe 1,8-anilinonaphthalene sulfonic acid (ANS). While significant differences were observed between levels of iodination in both the ANS binding and intrinsic fluorescence of the thyroglobulin, no significant differences in the near and far UV circular dichroism spectra of the protein as a function of iodine content were observed. These data suggest that, the iodination of thyroglobulin effects specific areas of the protein without significant disruption of its overall secondary structure.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zabel KM,Rawitch AB

doi

10.1016/0006-291x(84)90724-1

subject

Has Abstract

pub_date

1984-05-31 00:00:00

pages

310-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(84)90724-1

journal_volume

121

pub_type

杂志文章

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