Abstract
The binding of azide, thiocyanate, cyanate and cyanide to caeruloplasmin has been studied in detail. Comparative studies have also been made with laccase. The data are interpreted in terms of two binding sites per mole of caeruloplasmin, both sites involving copper(II), but only one site in laccase. On the basis of these data and previously reported studies of the copper enzymes a scheme for the reaction centres of caeruloplasmin is evolved. Stress is placed on the function of disulphide bridges.
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