Davies K J
Prog Clin Biol Res. 1985;195:15-27.
Human red blood cells (RBC) were exposed to oxygen-based free-radicals, and other activated oxygen species generated during incubation with xanthine plus xanthine oxidase (X+XO). Oxygen-radical exposure induced up to 30 fold increases in human RBC protein degradation, compared to 12 fold increases in rabbit RBC protein degradation. Protein degradation increased as a function of X+XO, but demonstrated saturation kinetics at higher XO concentrations. The presence or absence of an energy substrate (glucose) had no effect on protein degradation, indicating the possible role of ATP-independent proteinolytic systems. It is proposed that human RBC proteins can be oxidatively damaged by certain free-radicals, and that the oxidized proteins are specifically recognized and degraded by intracellular proteinolytic systems.
将人类红细胞（RBC）暴露于氧自由基以及在黄嘌呤与黄嘌呤氧化酶（X + XO）孵育过程中产生的其他活性氧物种中。与兔红细胞蛋白质降解增加12倍相比，氧自由基暴露导致人类红细胞蛋白质降解增加高达30倍。蛋白质降解随X + XO增加而增加，但在较高XO浓度下呈现饱和动力学。能量底物（葡萄糖）的存在与否对蛋白质降解没有影响，这表明非ATP依赖性蛋白水解系统可能发挥作用。有人提出，人类红细胞蛋白质可能会被某些自由基氧化损伤，并且氧化后的蛋白质会被细胞内蛋白水解系统特异性识别并降解。
