Iodination of Lysozyme

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Abstract
The differential iodination of tyrosine residues in the lysozyme [EC 3.2.1.17] molecule was investigated in consideration of their positions in the three dimensional structure of lysozyme crystal. One tyrosine residue was unreactive on iodination, while other two residues were stepwise iodinated. Under appropriate conditions, the two residues were iodinated completely to diiodotyrosine. The fractionation of iodinated lysozyme with CM-cellulose failed because of the deiodination of iodotyrosine by the adsorbent. From the measurement of the optical density at 320 mμ and spectro-photometric titration of iodinated lysozyme, it was concluded that the iodination controlled under appropriate conditions proceeded stepwise and homogeneously.

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