人类嗜酸性粒细胞中过氧化物酶的特性分析。
Characterization of the peroxidase in human eosinophils.
作者信息
Wever R, Hamers M N, de Graaf C J, Weening R S, Roos D
出版信息
Adv Exp Med Biol. 1982;141:501-9. doi: 10.1007/978-1-4684-8088-7_48.
Human eosinophil peroxidase is a cationic protein with a higher content of arginine, the enzyme being poorly soluble in water. The purified enzyme is able to carry out the peroxidative chlorination of monochlorodimedon. Like myeloperoxidase the position of the pH optimum of this reaction depends on the ration of the concentrations of chloride and H2O2. Compared to myeloperoxidase the pH optimum is shifted by 0.8 pH unit to more acid pH values. The physiological consequences of the properties of the eosinophil peroxidase are discussed.
人嗜酸性粒细胞过氧化物酶是一种精氨酸含量较高的阳离子蛋白，该酶在水中的溶解度较差。纯化后的酶能够对一氯二甲基酮进行过氧化氯化反应。与髓过氧化物酶一样，该反应的最适pH值位置取决于氯离子和过氧化氢浓度的比例。与髓过氧化物酶相比，最适pH值向更酸性的pH值方向偏移了0.8个pH单位。文中讨论了嗜酸性粒细胞过氧化物酶这些特性的生理意义。
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