酶促反应速率的压力变化:过氧化氢酶。

Physiological chemistry and physics Pub Date : 1981-01-01
E Morild, J E Olmheim
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引用次数: 0

摘要

用分光光度法和氧极谱法研究了压力对过氧化氢酶在1000 bar催化分解过氧化氢的影响。两种方法的比较表明,在700bar压力下,两种方法的一致性较好,但在700bar压力以上,偏差会增大。过氧化氢酶的动力学行为相当复杂,难以解释。当过氧化氢浓度较小时,反应速率随压力低于500巴而增加。对于较高的浓度,在所有压力下速率都减小。温度对压力行为没有显著影响,但KCl的加入使活化体积大幅增加。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Pressure variation of enzymatic reaction rates: III. Catalase.

The effect of pressure on the catalytic decomposition of hydrogen peroxide by catalase has been investigated to 1000 bar by spectrophotometry and oxygen polarography. Comparison between the two methods showed good agreement up to 700 bar but increasing deviation above that pressure. The kinetic behavior of catalase is rather complicated and difficult to interpret. For small peroxide concentrations the reaction rate increased with pressure below 500 bar. For higher concentrations the rate decreased at all pressures. Temperature had no marked effect on the pressure behavior but addition of KCl led to a large increase in activation volume.

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