Meban C
Histochemistry. 1975 Jun 9;43(4):367-72. doi: 10.1007/BF00490195.
The fine structural localization of nonspecific alkaline phosphatase was studied in the granular pneumonocytes (type II alveolar epithelial cells) of hamster lung by incubating sections of glutaraldehyde-fixed tissues in a medium containing lead ions and sodium beta-glycerophosphate or alpha-naphthyl acid phosphate. The specificity of the reaction was tested by exposing the sections to inhibitors of alkaline phosphatase. The results showed that alkaline phosphatase activity was present in the inclusion bodies of granular pneumonocytes. The enzyme reaction was strong in the membrane lining the inclusion bodies and a weaker reaction was generally detectable in the inclusion contents. Although only a proportion of the inclusion bodies showed enzyme activity, there was no obvious correlation between the reactivity of the inclusions and their intracellular position or size. The other organelles were unreactive. The finding of alkaline phosphatase activity within the inclusion bodies of granular pneumonocytes is an enigma as these organelles are generally considered to be lyosomes.
通过将戊二醛固定组织的切片置于含有铅离子和β-甘油磷酸钠或α-萘基磷酸的培养基中孵育，研究了仓鼠肺颗粒性肺细胞（II型肺泡上皮细胞）中非特异性碱性磷酸酶的精细结构定位。通过将切片暴露于碱性磷酸酶抑制剂来测试反应的特异性。结果显示，颗粒性肺细胞的包涵体内存在碱性磷酸酶活性。酶反应在包涵体的内膜中很强，而在包涵体内容物中通常可检测到较弱的反应。虽然只有一部分包涵体显示出酶活性，但包涵体的反应性与其细胞内位置或大小之间没有明显的相关性。其他细胞器无反应性。颗粒性肺细胞包涵体内存在碱性磷酸酶活性这一发现是一个谜，因为这些细胞器通常被认为是溶酶体。
