Abstract—It is established that a medium with a reduced content of deuterium has no effect on the secondary structure of horseradish peroxidase and bovine serum albumin and caused no conformational changes in the structures of these proteins. The placement of these proteins in a buffer solution prepared based on deuterium-depleted water led to a decrease in the intensity of intrinsic tryptophan fluorescence, while the circular dichroism spectra remained virtually unchanged. A decrease in the content of deuterium in the reaction medium led to a decrease in the activity of the peroxidase oxidation reaction of o-dianisidine and luminal with hydrogen peroxide.

中文翻译：

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不同同位素2 H / 1 H组成的培养基中辣根过氧化物酶和牛血清白蛋白功能活性的变化

摘要—已确定氘含量降低的培养基对辣根过氧化物酶和牛血清白蛋白的二级结构没有影响，并且不会引起这些蛋白质结构的构象变化。这些蛋白质在基于贫氘水制备的缓冲溶液中的放置导致固有色氨酸荧光强度的降低，而圆二色性光谱实际上保持不变。反应介质中氘含量的减少导致邻二苯胺和过氧化氢与管腔的过氧化物酶氧化反应的活性降低。