Konat G W, Wiggins R C
J Neurochem. 1985 Oct;45(4):1113-8. doi: 10.1111/j.1471-4159.1985.tb05530.x.
Fresh myelin, isolated from brainstems of adult rats, was incubated in the presence of Cu2+ and H2O2. Electrophoretic analysis of the reisolated myelin membrane revealed a gradual loss of the protein moiety from the characteristic pattern and an increase in aggregated material appearing at the origin of the gel. The aggregation of proteins was time-dependent and was concomitant with the accumulation of lipid peroxidation products reactive with thiobarbituric acid. Furthermore, during the course of incubation, there was a gradual decrease in the amount of recovered light myelin and a quantitatively similar increase in heavier myelin subfractions. The aggregation of proteins seems not to be directly related to the buoyant densities of myelin fragments. The peroxidative damage to the myelin proteins may be an important contributor to pathochemistry of myelin sheath, in particular, and in general it implies the susceptibility of the protein moiety of cell membranes to oxygen-induced deterioration.
从成年大鼠脑干分离出的新鲜髓磷脂在铜离子（Cu2+）和过氧化氢（H2O2）存在的情况下进行孵育。对重新分离的髓鞘膜进行电泳分析显示，蛋白质部分从特征模式逐渐丢失，并且在凝胶原点处出现的聚集物质增加。蛋白质的聚集是时间依赖性的，并且与与硫代巴比妥酸反应的脂质过氧化产物的积累同时发生。此外，在孵育过程中，回收的轻髓磷脂量逐渐减少，而较重的髓磷脂亚组分在数量上有类似的增加。蛋白质的聚集似乎与髓磷脂片段的浮力密度没有直接关系。髓磷脂蛋白的过氧化损伤可能是髓鞘病理化学的一个重要因素，特别是，一般来说，这意味着细胞膜蛋白质部分对氧诱导的降解敏感。
