Greiten H, Rister M, Steigleder G K
Department of Dermatology, University of Cologne, Köln, Federal Republic of Germany.
Arch Dermatol Res. 1987;279 Suppl:S63-5. doi: 10.1007/BF00585923.
The specific activity of myeloperoxidase (MPO), an enzyme located in the primary granules of polymorphonuclear leukocytes, was measured in patients with psoriasis vulgaris and compared with that in patients with atopic dermatitis and in healthy subjects. MPO catalyzes the oxidation of guaiacol into tetraguaiacol in the presence of H2O2. The activity was determined by photometric measurement of tetraguaiacol. The specific MPO activity showed no statistically significant difference between the healthy subjects and the patients with atopic dermatitis. In comparison to these two groups the specific MPO activity of the psoriatic patients showed a slight reduction which was, however, not statistically significant.
测定了寻常型银屑病患者中髓过氧化物酶（MPO，一种位于多形核白细胞初级颗粒中的酶）的比活性，并与特应性皮炎患者及健康受试者的比活性进行了比较。MPO在过氧化氢存在的情况下催化愈创木酚氧化为四愈创木酚。通过对四愈创木酚进行光度测量来确定活性。健康受试者和特应性皮炎患者之间的MPO比活性无统计学显著差异。与这两组相比，银屑病患者的MPO比活性略有降低，但无统计学显著意义。
