Russo J, Wells P
J Histochem Cytochem. 1977 Feb;25(2):135-48. doi: 10.1177/25.2.138706.
Adenosine triphosphatase (ATPase) activity was localized at an ultrastructural level in the resting mammary glands of female BALB/c mice. A Mg++ dependent ATPase was localized in the plasma membranes of both the epithelial and myoepithelial cells of the mammary tubules. A second type of ATPase activity that was not Mg++-dependent but that was Na+ and K+ dependent was localized primarily in the plasma membranes of the myoepithelial cells. Preincubation with either ouabain or N-ethylmaleimide decreased the quantity of reaction product, indicating that both types of ATPase activity were sensitive to these inhibitors. Control media, containing adenosine triphosphate and Pb(NO3)2 without cations, demonstrated that the amount of nonezymatic hydrolysis was negligible. These differences in the cationic requirements for plasma membrane ATPase activity can be used to distinguish histochemically the epithelial from myoepithelial cells in mammary tissue.
在雌性BALB/c小鼠的静止乳腺中，三磷酸腺苷酶（ATPase）活性定位在超微结构水平。一种依赖Mg++的ATP酶定位在乳腺小管上皮细胞和肌上皮细胞的质膜中。第二种类型的ATP酶活性不依赖Mg++，但依赖Na+和K+，主要定位在肌上皮细胞质膜中。用哇巴因或N-乙基马来酰亚胺预孵育会减少反应产物的量，表明这两种类型的ATP酶活性对这些抑制剂敏感。含有三磷酸腺苷和无阳离子的Pb(NO3)2的对照培养基表明，非酶水解量可忽略不计。质膜ATP酶活性对阳离子需求的这些差异可用于在组织化学上区分乳腺组织中的上皮细胞和肌上皮细胞。
