Abstract
ABSTRACT In vivo 125I-labelled dog thyroglobulin was either extracted with acid acetone or subjected to gel filtration, in order to see whether the iodoaminoacids could be removed. The acetone extracts or the material adsorbed on to the Sephadex columns contained 5–16% of the total 125I-activity present in the purified protein. These fractions of radioactivity were analyzed by two dimensional chromatography and iodoaminoacids found to be present. By equilibrium experiments it was further shown that our thyroglobulin preparation would only bind thyroxine but not 3-mono- and 3,5-diiodotyrosine. A possible interpretation of these results is that at least a fraction of the iodinated compounds of thyroglobulin is linked to the protein by non-covalent bonds.
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