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[在尿素和酸性pH值作用下活力青霉过氧化氢酶的解离]

[Dissociation of Penicillium vitale catalase under the effect of urea and acid pH].

作者信息

Mironenko N I, Protvin D D, Degtiar R G, Guliĭ M F

出版信息

Ukr Biokhim Zh. 1977 May-Jun;49(3):94-8.

PMID:18833
Abstract

Conditions are studied for Penicillium vitale catalase dissociation into subunits under the effect of urea (0.7-8.5 M) and acid pH (5.0-2.0). In 8.0 M urea (pH 5.0) a molecule of the P. vitale catalase dissociates with formation of the components, the sedimentation coefficient of which is 2.4+/-0.2S, the molecular weight is 153000+/-2800. Dissociation at pH 2.2 in 4.0 M urea results in formation of components with the sedimentation coefficient 2.2+/-0.3 S. The catalase molecule dissociation under the mentioned conditions is accompanied by a loss in the enzyme activity. The results obtained show that dissociation of the P. vitale catalase molecule requires more rigid conditions than dissociation of the animal catalase. At the same time the catalase after dissociation in 8.0-8.5 M urea loses its ability to reassociation with a decrease in the urea concentration up to 0.08 M.

摘要

研究了在尿素(0.7 - 8.5 M)和酸性pH(5.0 - 2.0)作用下,活力青霉过氧化氢酶解离为亚基的条件。在8.0 M尿素(pH 5.0)中,活力青霉过氧化氢酶分子解离形成组分,其沉降系数为2.4±0.2 S,分子量为153000±2800。在4.0 M尿素中pH 2.2条件下解离会形成沉降系数为2.2±0.3 S的组分。上述条件下过氧化氢酶分子的解离伴随着酶活性的丧失。所得结果表明,活力青霉过氧化氢酶分子的解离比动物过氧化氢酶的解离需要更严格的条件。同时,在8.0 - 8.5 M尿素中解离后的过氧化氢酶,当尿素浓度降至0.08 M时,失去了重新结合的能力。

相似文献

3
[Study of the subunit structure of catalase from Penicillium vitale].
Ukr Biokhim Zh (1978). 1985 Jul-Aug;57(4):29-33.
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[The kinetic and catalytic properties of Penicillium vitale catalase].
Ukr Biokhim Zh (1978). 1996 Mar-Apr;68(2):69-73.

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