Beck-Speier I, Leuschel L, Luippold G, Maier K L
Projekt Inhalation der Gesellschaft für Strahlen- und Umweltforschung München, Arbeitsgruppe Biochemie, Neuherberg, FRG.
FEBS Lett. 1988 Jan 18;227(1):1-4. doi: 10.1016/0014-5793(88)81401-7.
In proteins released from quiescent human neutrophils during incubation, 21% of the methionine (Met) residues were found to be oxidized. However, the portion of oxidized Met in extracellular proteins increased to 66% after stimulating the cells with zymosan and to 75% after stimulation with phorbol myristate acetate (PMA). Generation of such high levels of oxidized Met in native proteins by activated neutrophils has, so far, not been observed. The presence of superoxide dismutase during incubation of PMA-stimulated cells produced a negligible effect on methionine oxidation, while the presence of catalase resulted in a methionine sulfoxide (Met(O)) content of only 28% in the released proteins. It is proposed that the conversion of Met to Met(O) in these proteins predominantly occurs by action of the myeloperoxidase/H2O2/Cl- system in the extracellular space.
在静息人中性粒细胞孵育期间释放的蛋白质中，发现21%的甲硫氨酸（Met）残基被氧化。然而，在用酵母聚糖刺激细胞后，细胞外蛋白质中氧化Met的比例增加到66%，在用佛波酯肉豆蔻酸酯（PMA）刺激后增加到75%。迄今为止，尚未观察到活化的中性粒细胞在天然蛋白质中产生如此高水平的氧化Met。在PMA刺激的细胞孵育期间超氧化物歧化酶的存在对甲硫氨酸氧化产生的影响可忽略不计，而过氧化氢酶的存在导致释放的蛋白质中甲硫氨酸亚砜（Met（O））含量仅为28%。有人提出，这些蛋白质中Met向Met（O）的转化主要通过细胞外空间中的髓过氧化物酶/H2O2/Cl-系统的作用发生。
