Petrali E H, Sulakhe P V
Enzyme. 1980;25(2):102-5. doi: 10.1159/000459227.
Myelin isolated from the peripheral (PNS) and central nervous system (CNS) of mouse contained a protein kinase which catalyzed phosphorylation of myelin proteins. In the case of CNS myelin, small and large basic proteins were phosphorylated whereas in the case of PNS myelin, a glycoprotein (Po) as well as other basic proteins (P1 and P2) were phosphorylated. Ca2+, but not adenosine 3',5'-monophosphate (cyclic AMP), markedly (5- to 10-fold) stimulated phosphorylation of PNS and CNS myelin proteins. There was no difference between the normal and dystrophic mouse CNS myelin phosphorylation. However, a marked decrease in the cauda equina PNS myelin phosphorylation ofthe dystrophic mouse was observed. Interestingly, the dystrophic sciatic nerve myelin phosphorylation, compared to normal, was higher.
从小鼠外周神经系统（PNS）和中枢神经系统（CNS）分离出的髓磷脂含有一种蛋白激酶，该激酶可催化髓磷脂蛋白的磷酸化。就中枢神经系统髓磷脂而言，小碱性蛋白和大碱性蛋白会发生磷酸化，而在外周神经系统髓磷脂中，一种糖蛋白（Po）以及其他碱性蛋白（P1和P2）会发生磷酸化。Ca2+而非3',5'-单磷酸腺苷（环磷酸腺苷）能显著（5至10倍）刺激外周神经系统和中枢神经系统髓磷脂蛋白的磷酸化。正常小鼠和营养不良小鼠的中枢神经系统髓磷脂磷酸化之间没有差异。然而，观察到营养不良小鼠马尾外周神经系统髓磷脂的磷酸化显著降低。有趣的是，与正常情况相比，营养不良的坐骨神经髓磷脂磷酸化更高。
