Abstract
Oral administration of 2-thiouracil, for periods up to 28 days, greatly affected the soluble proteins of the rat thyroid gland. After 2 days, the iodine/protein ratio declined to less than half that present in the normal group. Ultracentrifugal analyses of the thyroid extracts showed a decrease in the 19 S thyroglobulin component, and a progressive increase in the 3 S component. After 7 days of treatment with 2-thiouracil, the 3 S component was the major protein constituent. The 11 S component rose to a maximum at 7 days and subsequently declined. Chromatographic fractionation of some of the thyroid extracts on Sephadex G-200 revealed similar changes in protein distributions. Both the whole thyroid extracts and their Sephadex G-200 fractions were examined by immunoelectrophoresis and the 19 S, 11 S, and 3 S components were characterized as having electrophoretic mobilities in the albumin-α1, α2, and α1-β regions respectively. By the micro-Ouchterlony agar gel technique, the 3 S component did not cross-react with the 19 S or 11 S components. In addition, the 19 S and (or) 11 S components of the 14-day group showed only partial cross-reaction with those of the normal group.
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