Xu L, Li C, Wu Q, Wang B
Hua Xi Yi Ke Da Xue Xue Bao. 1990 Sep;21(3):256-8.
Myeloperoxidase (MPO) plays an important role in the oxygen-dependent microbicidal mechanism of polymorphonuclear neutrophils. The purpose of our study was to investigate the therapeutic potency of human MPO preparations. This paper is to present our work on MPO purification and its identification. White blood cells, isolated freshly from normal donors, were lysed with cetyltrimethylammonium bromide to liberate myeloperoxidase. The purified MPO was obtained by 65% (NH4)2SO4 precipitation followed by separation over the Sephadex G150 column. These pure MPO preparations were green in color and had an A430/A280 nm of 0.68. The enzymatic activity was of 29.77 u/mg. The pure normal MPO was composed of a 59,000 MW peptide, a 13,500 MW peptide, and a 38,000 MW peptide when subjected to SDS-PAGE under reducing conditions. The study of the therapeutic effect of the pure MPO on mice with C. albicans infection is under way.
髓过氧化物酶（MPO）在多形核中性粒细胞的氧依赖性杀菌机制中发挥着重要作用。我们研究的目的是探究人MPO制剂的治疗效力。本文将展示我们在MPO纯化及其鉴定方面的工作。从正常供体新鲜分离的白细胞用十六烷基三甲基溴化铵裂解以释放髓过氧化物酶。通过65%硫酸铵沉淀，随后在葡聚糖凝胶G150柱上分离获得纯化的MPO。这些纯MPO制剂呈绿色，A430/A280 nm为0.68。酶活性为29.77 u/mg。在还原条件下进行SDS-PAGE时，纯正常MPO由一个59,000 MW的肽、一个13,500 MW的肽和一个38,000 MW的肽组成。关于纯MPO对白色念珠菌感染小鼠治疗效果的研究正在进行中。
