Inomata K, Yoshioka T, Nasu F, Mayahara H
Acta Anat (Basel). 1984;118(4):243-8. doi: 10.1159/000145852.
The ultracytochemical localization of eight hydrolytic enzymes (TMPase, 5'-NPase, TPPase, TTPase, Mg++-ATPase, Ca++-ATPase, ALPase and K+-NPPase) and one oxidative enzyme (MAO) was determined in rat brain capillary endothelial cells. In the somal plasma membrane, the enzymatic activity was mainly located in the antiluminal plasma membrane. This finding was appropriate for enzymes possessing the optimal pH at alkaline ranges, except for alkaline phosphatase. Most enzymes investigated showed a positive reaction on the pinocytotic vesicles of capillary endothelial cells. Differences in the intensity of the enzyme activities of the luminal and antiluminal plasma membranes may reflect the polarity in the capillary endothelial cells and relate to blood-brain barrier mechanisms.
在大鼠脑毛细血管内皮细胞中测定了八种水解酶（TMPase、5'-NPase、TPPase、TTPase、Mg++-ATPase、Ca++-ATPase、ALPase和K+-NPPase）和一种氧化酶（MAO）的超细胞化学定位。在胞体的质膜中，酶活性主要位于反腔质膜。这一发现适用于在碱性范围内具有最佳pH值的酶，但碱性磷酸酶除外。大多数研究的酶在毛细血管内皮细胞的胞饮小泡上呈阳性反应。腔质膜和反腔质膜酶活性强度的差异可能反映了毛细血管内皮细胞的极性，并与血脑屏障机制有关。
