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J. Biochem, 1968, Vol. 64, No. 2 239-245
© 1968 Japanese Biochemical Society

research-article

Iodination of Lysozyme

I. Differential Iodination of Tyrosine Residues

KATSUYA HAYASHI, TADAHISA SHIMODA, KATSUHIKO YAMADA*, AKIHIKO KUMAI** and MASARU FUNATSU

From the Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University Fukuoka

The differential iodination of tyrosine residues in the lysozyme [EC 3.2.1.17 [EC] ] 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.

*Present address: * Kirin Beer Co. Ltd., Takasaki

**Present address: * Teikoku-zoki Co. Ltd., Kawasaki.


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