Abstract
1. 1. The iodination of casein and thyroglobulin under various conditions results in a progressive diminution of the tryptophan contents as estimated by Lugg's method, the application of which to iodinated proteins has been worked out. The observations can be explained in terms of either an iodinated derivative of tryptophan or its oxidation. 2. 2. The de-iodination of halogenated proteins by sodium stannite liberates tyrosine and monoiodotyrosine from di-iodotyrosine, but the reaction does not liberate any tryptophan from iodoproteins. It is thus improbable that these proteins contain an iodo-tryptophan. 3. 3. Tryptophan treated with iodine in neutral or slightly alkaline solutions is oxidised without previous substitution, the iodine being reduced quantitatively in hydriodic acid. This is most likely to happen also in proteins, in which tyrosine and histidine are the only amino acids liable to be iodinated in important amounts.
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