Literature DB >> 16749096

An investigation of the decolorization of caeruloplasmin by acid.

G Curzon1.   

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.

Entities:  

Year:  1965        PMID: 16749096      PMCID: PMC1264555          DOI: 10.1042/bj0970151

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  16 in total

1.  Quantitative electron spin resonance studies on native and denatured ceruloplasmin and laccase.

Authors:  L BROMAN; B G MALMSTROM; R AASA; T VANNGARD
Journal:  J Mol Biol       Date:  1962-09       Impact factor: 5.469

2.  Monoamine oxidase. II. Copper, one of the prosthetic groups of plasma monoamine oxidase.

Authors:  H YAMADA; K T YASUNOBU
Journal:  J Biol Chem       Date:  1962-10       Impact factor: 5.157

3.  Purification and properties of a blue protein from etiolated mung bean seedlings.

Authors:  H SHICHI; D P HACKETT
Journal:  Arch Biochem Biophys       Date:  1963-02       Impact factor: 4.013

4.  Physical and chemical studies on ceruloplasmin. I. The relation between blue color and the valence states of copper.

Authors:  W E BLUMBERG; J EISINGER; P AISEN; A G MORELL; I H SCHEINBERG
Journal:  J Biol Chem       Date:  1963-05       Impact factor: 5.157

5.  Physicochemical studies of human ceruloplasmin.

Authors:  C B KASPER; H F DEUTSCH
Journal:  J Biol Chem       Date:  1963-07       Impact factor: 5.157

6.  The effects of some ions and chelating agents on the oxidase activity of caeruloplasmin.

Authors:  G CURZON
Journal:  Biochem J       Date:  1960-10       Impact factor: 3.857

7.  The chemistry and biochemistry of caeruloplasmin.

Authors:  G CURZON
Journal:  Proc R Soc Med       Date:  1959-01

8.  The purification of human caeruloplasmin.

Authors:  G CURZON; L VALLET
Journal:  Biochem J       Date:  1960-02       Impact factor: 3.857

9.  Purification and physico-chemical properties of laccase.

Authors:  T NAKAMURA
Journal:  Biochim Biophys Acta       Date:  1958-10

10.  Enzyme-metal-substrate complexes as co-ordination compounds.

Authors:  L E ORGEL
Journal:  Biochem Soc Symp       Date:  1958
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  1 in total

1.  The inhibition of caeruloplasmin by azide.

Authors:  G Curzon
Journal:  Biochem J       Date:  1966-08       Impact factor: 3.857

  1 in total

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