Safadi A, Livne E, Silbermann M, Reznick A Z
Laboratory for Musculoskeletal Research, Rappaport Family Institute for Research, Haifa, Israel.
J Histochem Cytochem. 1991 Feb;39(2):199-203. doi: 10.1177/39.2.1987264.
Alkaline phosphatase (AP), a membrane-associated glycoprotein which enhances the hydrolysis of monophosphate esters at alkaline pH, is widely distributed in animal tissues. AP activity is increased in a variety of muscle disorders, i.e., myopathies and denervation. Established histochemical methods at the light microscopy level failed to demonstrate AP in skeletal muscles. In the present study we applied the Gomori lead nitrate method for ultrastructural examination of AP in rat gastrocnemius muscles and showed that the enzyme was linked to the sarcolemma of the striated muscle and to the membranes of endothelial cells in adjacent capillaries. In comparison with ATPase activity, AP activity was inhibited by both levamisole and a pH of 7.2, but not by ouabain. Hence, it appears that in skeletal muscles AP is active at a high pH and is bound to cell membranes.
碱性磷酸酶（AP）是一种与膜相关的糖蛋白，可增强碱性pH下单磷酸酯的水解，广泛分布于动物组织中。在多种肌肉疾病（即肌病和去神经支配）中，AP活性会增加。在光学显微镜水平上已建立的组织化学方法未能在骨骼肌中显示出AP。在本研究中，我们应用Gomori硝酸铅法对大鼠腓肠肌中的AP进行超微结构检查，结果表明该酶与横纹肌的肌膜以及相邻毛细血管内皮细胞的膜相关。与ATPase活性相比，左旋咪唑和pH值为7.2均能抑制AP活性，但哇巴因不能。因此，似乎在骨骼肌中AP在高pH下具有活性并与细胞膜结合。
