Agrawal H C, Agrawal D, Yoshimura T, Benjamins J A
Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110.
Neurochem Res. 1987 Sep;12(9):783-6. doi: 10.1007/BF00971515.
Both proteolipid proteins (PLP) and DM-20 were found to be present by the immunoblot technique in myelin isolated from quaking mouse brain; however, the relative concentration of these proteins in myelin from quaking brain was substantially reduced when compared to the control. Brain slices from littermate control and quaking mice were incubated with [3H]palmitic acid to determine the incorporation of fatty acid into myelin proteolipid proteins. Fluorography of gels containing myelin proteins from control and quaking mice brain revealed that both PLP and DM-20 were acylated. The incorporation of [3H]palmitic acid into quaking myelin PLP and DM-20 was reduced by 75% and 20% respectively of those in control brain. The significance of differential acylation of quaking myelin PLP and DM-20 is discussed with respect to availability of non-acylated pools of proteolipid proteins and the activities of acylating enzymes.
通过免疫印迹技术发现，震颤小鼠脑分离出的髓磷脂中存在蛋白脂质蛋白（PLP）和DM-20；然而，与对照组相比，震颤脑髓磷脂中这些蛋白的相对浓度大幅降低。将同窝对照小鼠和震颤小鼠的脑切片与[3H]棕榈酸一起孵育，以确定脂肪酸掺入髓磷脂蛋白脂质蛋白的情况。对含有对照小鼠和震颤小鼠脑髓磷脂蛋白的凝胶进行荧光显影，结果显示PLP和DM-20都被酰化。与对照脑相比，[3H]棕榈酸掺入震颤髓磷脂PLP和DM-20的量分别减少了75%和20%。文中就蛋白脂质蛋白非酰化库的可用性和酰化酶的活性，讨论了震颤髓磷脂PLP和DM-20酰化差异的意义。
