Peterson R G, Gruener R W
Brain Res. 1978 Aug 18;152(1):17-29. doi: 10.1016/0006-8993(78)90131-2.
The localization of PNS myelin protein was studied using two methods: (1) lactoperoxidase catalysed iodination of intraperiod band material, (2) solubilization of basic proteins with ammonium acetate--Triton X-100 solutions. When myelin was swollen in the presence of lactoperoxidase and subsequently submitted to lactoperoxidase catalysed iodination P0 and what appeared to be the X protein labeled with 125I. In specimens which were disrupted in 50% ethyl alcohol, the basic proteins P1 and P2 were also iodinated. When the lactoperoxidase was omitted, there was no labeling of proteins. Ammonium acetate--Triton X-100 solutions solubilized basic proteins from both whole nerve and purified myelin preparations. Electron microscopic changes which accompanied this modification included swelling and splitting of the main period band. These data indicate that the P0 and X proteins are available for iodination in the intraperiod band of swollen PNS myelin and that basic proteins are localized in the main period band.
（1）乳过氧化物酶催化周期带内物质的碘化；（2）用醋酸铵 - 曲拉通X - 100溶液溶解碱性蛋白。当髓磷脂在乳过氧化物酶存在下膨胀，随后进行乳过氧化物酶催化的碘化时，P0以及似乎是X蛋白被125I标记。在50%乙醇中破坏的标本中，碱性蛋白P1和P2也被碘化。当省略乳过氧化物酶时，蛋白质没有标记。醋酸铵 - 曲拉通X - 100溶液可溶解来自全神经和纯化髓磷脂制剂的碱性蛋白。伴随这种修饰的电子显微镜变化包括主周期带的肿胀和分裂。这些数据表明，P0和X蛋白在肿胀的周围神经系统髓磷脂的周期带内可用于碘化，并且碱性蛋白定位于主周期带。
