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引用本文的文献

1
The inhibition of caeruloplasmin by azide.叠氮化物对铜蓝蛋白的抑制作用。
Biochem J. 1966 Aug;100(2):295-302. doi: 10.1042/bj1000295.

本文引用的文献

1
The influence of temperature and pH upon the rate of denaturation of ricin.温度和pH值对蓖麻毒素变性速率的影响。
J Biol Chem. 1950 Oct;186(2):829-47.
2
Studies on laccases of lacquer trees. IV. Purification and properties of a blue protein obtained from latex of Rhus vernicifera.漆树漆酶的研究。IV. 从漆树胶乳中获得的一种蓝色蛋白质的纯化及性质
J Biochem. 1961 Nov;50:394-9. doi: 10.1093/oxfordjournals.jbchem.a127465.
3
Isolation and properties of a beta-mercaptopyruvate-cleaving copper enzyme.一种β-巯基丙酮酸裂解铜酶的分离与性质
Biochim Biophys Acta. 1959 Apr;32:338-48. doi: 10.1016/0006-3002(59)90605-5.
4
PHYSICAL AND CHEMICAL STUDIES ON CERULOPLASMIN. II. MOLECULAR OXYGEN AND THE BLUE COLOR OF CERULOPLASMIN.
J Biol Chem. 1964 Apr;239:1042-3.
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RECONSTITUTION OF ACID-DENATURED CATALASE.酸变性过氧化氢酶的复性
J Biol Chem. 1963 Oct;238:3256-61.
6
Reversible decolorisation of caeruloplasmin under acid conditions.在酸性条件下铜蓝蛋白的可逆脱色
Biochim Biophys Acta. 1963 Apr 2;71:249-50. doi: 10.1016/0006-3002(63)91078-3.
7
Quantitative electron spin resonance studies on native and denatured ceruloplasmin and laccase.天然和变性铜蓝蛋白及漆酶的定量电子自旋共振研究。
J Mol Biol. 1962 Sep;5:301-10. doi: 10.1016/s0022-2836(62)80074-6.
8
Monoamine oxidase. II. Copper, one of the prosthetic groups of plasma monoamine oxidase.单胺氧化酶。II. 铜,血浆单胺氧化酶的辅基之一。
J Biol Chem. 1962 Oct;237:3077-82.
9
Purification and properties of a blue protein from etiolated mung bean seedlings.来自黄化绿豆幼苗的一种蓝色蛋白质的纯化及性质
Arch Biochem Biophys. 1963 Feb;100:185-91. doi: 10.1016/0003-9861(63)90060-2.
10
Physical and chemical studies on ceruloplasmin. I. The relation between blue color and the valence states of copper.铜蓝蛋白的物理和化学研究。I. 蓝色与铜价态之间的关系。
J Biol Chem. 1963 May;238:1675-82.

酸对血浆铜蓝蛋白脱色作用的研究。

An investigation of the decolorization of caeruloplasmin by acid.

作者信息

Curzon G

机构信息

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

出版信息

Biochem J. 1965 Oct;97(1):151-7. doi: 10.1042/bj0970151.

DOI:10.1042/bj0970151
PMID:16749096
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1264555/
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.
摘要
  1. 在不同温度和pH值条件下研究了铜蓝蛋白的酸脱色作用。2. 可区分出两种脱色反应:(i) 具有蛋白质变性热力学特征的不可逆反应;(ii) 在25摄氏度时铜蓝蛋白的蓝色和无色形式之间达到平衡,表观pK为3.7。3. 平衡的低温依赖性表明它不涉及总体变性变化。4. 可逆脱色在有氧和无氧条件下均会发生,表明该变化不涉及铜-氧复合物的解离。5. 描述了脱色过程中的光谱变化。6. 结合铜蓝蛋白总体结构的形式模型讨论了酸脱色过程中发生的变化。