Abstract
Circular dichroism spectra between 300 and 1100 nm are presented for stellacyanin, Rhus vernicifera laccase, Polyporus versicolor laccase and human ceruloplasmin. The number of bands in this region varies between four and six for the different proteins. In addition to these bands some unresolved ellipticity is present between 350 to 400 nm. It is shown that all these bands are associated with the blue chromophore. The effect of azide on ceruloplasmin is studied with optical and circular dichroism spectroscopy. The results are not fully interpreted but it is concluded that the decrease of the blue colour cannot be explained simply by reduction of copper.
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