Edwards A M, Ross N W, Ulmer J B, Braun P E
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
J Neurosci Res. 1989 Jan;22(1):97-102. doi: 10.1002/jnr.490220113.
The interaction of myelin basic protein (MBP) and proteolipid protein (PLP) was studied using a microtitre well binding assay and the ligand-blot overlay technique. The binding of iodinated PLP to MBP that was immobilized on microtitre wells was saturable and reversible. Its selectivity was investigated by the ligand-blot overlay technique. Iodinated PLP was found to bind MBP but not any other CNS myelin proteins. This interaction was not dependent on the phosphoryl moiety of MBP. Binding of PLP to histone H4 also occurred, but the amount of PLP bound per unit MBP was greater than for this histone.
使用微量滴定孔结合试验和配体印迹覆盖技术研究了髓鞘碱性蛋白（MBP）与蛋白脂质蛋白（PLP）的相互作用。碘化PLP与固定在微量滴定孔上的MBP的结合是可饱和且可逆的。通过配体印迹覆盖技术研究了其选择性。发现碘化PLP可与MBP结合，但不与任何其他中枢神经系统髓鞘蛋白结合。这种相互作用不依赖于MBP的磷酸基团。PLP与组蛋白H4也会发生结合，但每单位MBP结合的PLP量比与该组蛋白结合的量更多。
