Biochem J. 1965 Oct;97(1):151-7.

An investigation of the decolorization of caeruloplasmin by acid.

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Department of Chemical Pathology, Institute of Neurology, The National Hospital, Queen Square, London, W.C.1.

Abstract

1. The acid decolorization of caeruloplasmin was studied at various temperatures and pH values. 2. Two decolorization reactions may be distinguished: (i) an irreversible reaction with the thermodynamic characteristics of a protein denaturation; (ii) the attainment of an equilibrium between blue and colourless forms of caeruloplasmin with apparent pK 3.7 at 25 degrees . 3. The low temperature-dependence of the equilibrium suggests that it does not involve a gross denaturative change. 4. The reversible decolorization occurred both aerobically and anaerobically, indicating that the change does not involve dissociation of a copper-oxygen complex. 5. Spectral changes during the decolorization are described. 6. The changes occurring during acid decolorization are discussed in relation to a formal model of the gross structure of caeruloplasmin.

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The inhibition of caeruloplasmin by azide. [Biochem J. 1966]
The inhibition of caeruloplasmin by azide.
Curzon G. Biochem J. 1966 Aug; 100(2):295-302.

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An investigation of the decolorization of caeruloplasmin by acid.

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