Abstract
1. 1.|The conformations of rabbit creatine kinase and some kinases from invertebrates have been studied and compared by circular dichroism between 320 and 185 nm. 2. 2.|All these enzymes present the same dichroic pattern between 250 and 185 nm, suggesting that they have similar secondary and tertiary structures. 3. 3.|The optical activity of their side-chain chromophores is small. However, the comparison of their ellipticity bands between 300 and 250 nm allows us to distinguish a different tyrosine local environment for each enzyme. 4. 4.|In the lobster arginine kinase the ellipticity bands disappear in the region of aromatic chromophores after alkalinisation or nitration of its four accessible tyrosyl residues. This loss of optical activity is discussed in relation to the conformational alterations following such chemical modifications.
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