Kanoh N, Kumoi T
Department of Otolaryngology, Hyogo College of Medicine, Japan.
ORL J Otorhinolaryngol Relat Spec. 1994 May-Jun;56(3):143-5. doi: 10.1159/000276630.
The localization of ouabain-sensitive, K(+)-dependent p-nitrophenylphosphatase (K-NPPase) activity, the second dephosphorylative property of the Na-K adenosine triphosphatase complex, was cytochemically studied in the intra-temporal portion of the facial nerve in normal guinea pigs using a cerium-based method. A fine-granular reaction product of the K-NPPase activity was observed on the cytoplasmic side of the axolemma of the axon cylinder, of the incisures of Schmidt-Lanterman, and of the nodes of Ranvier. No reaction product was detected on the periaxonal and outermost plasma membrane of Schwann cells and in the myelin sheath. In control tissue samples, the enzyme activity was almost completely inhibited by 10 mM ouabain, and no reaction was noted in medium without K+.
采用铈基方法，对正常豚鼠面神经颞内段钠钾三磷酸腺苷酶复合物的第二种去磷酸化特性——哇巴因敏感的、钾离子依赖的对硝基苯磷酸酶（K-NPPase）活性进行了细胞化学定位研究。在轴索圆柱体的轴膜、施密特-兰特尔曼切迹和郎飞结的胞质侧观察到K-NPPase活性的细颗粒反应产物。在施万细胞的轴周和最外层质膜以及髓鞘中未检测到反应产物。在对照组织样本中，10 mM哇巴因几乎完全抑制了酶活性，在无钾离子的培养基中未观察到反应。
