The presence of an iodinated albumin in the soluble thyroid proteins of rat has been shown after labeling with radioactive iodine the thyroid glands in vivo or in vitro.
The purification of this protein fraction was carried out by centrifugation on sucrose gradient followed by filtration on Sephadex G-200.
The purified iodoprotein migrates as an albumin in starch-gel or disc electrophoresis. It is immunoelectrophoretically identical to serumalbumin. It contains MIT, DIT and the hormones (T4, T3). After a short pulse with radioactive iodine in vivo or in vitro, its specific radioactivity is much higher than that of S19 thyroglobulin or other thyroglobulin-like proteins. It is concluded that the thyroid gland of normal rat contains (and most probably synthetizes) an albumin which is able to be iodinated and to contribute to the synthesis of thyroid hormones. In conditions where the synthesis of thyroglobulin is impaired, this iodoalbumin might represent the main substrate for thyroid hormone biosynthesis.
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