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过氧化氢酶的热稳定性和pH依赖性:一项比较研究

Heat and pH dependence of catalase. A comparative study.

作者信息

Góth L

机构信息

Laboratory Division, Municipal Hospital, Sümeg, Hungary.

出版信息

Acta Biol Hung. 1987;38(2):279-85.

PMID:3454087
Abstract

Effects of pH and heat were examined on the activity of enzyme catalase from human sources (normal and pathological sera, tissue homogenates, purified catalases). The pH optimum, temperature optimum and T50 values of purified catalases were lower than those of normal, or pathological sera and tissue homogenates. On contrast, the activation energy showed its highest value in purified catalase. These findings might be explained by the post-translational modification of enzyme catalase. The obtained results failed to enhance the diagnostic role of serum catalase determination, nevertheless, gave the optimal values of pH and temperature for catalase assay.

摘要

研究了pH值和温度对人源过氧化氢酶活性的影响(正常和病理血清、组织匀浆、纯化的过氧化氢酶)。纯化的过氧化氢酶的最适pH值、最适温度和T50值低于正常或病理血清及组织匀浆。相反,纯化的过氧化氢酶的活化能最高。这些发现可能是由于过氧化氢酶的翻译后修饰。所得结果未能增强血清过氧化氢酶测定的诊断作用,但给出了过氧化氢酶测定的最佳pH值和温度。

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