Osipova E A
Arkh Anat Gistol Embriol. 1976;71(11):85-8.
The results of detection of phosphatases with different substrates in the cells forming steroid hormones in ovaries, testes and adrenals of newborn seals, ovaries of adult seals and adrenals of adult rabbits, dogs and man were compared. The first group of substrates includes sodium glycerophosphate, glucose-1-phosphate, nitrophenylphosphate (Gomori's sulfide method). The second group includes naphthol phosphates AS-BI, AS-MX and AS-BS, whose hydrolysis is determined by simultaneous and successive azocoupling with diazotized benzidine and stable diazotates by fast blue and fast cherry-coloured. Detection of phosphomonesterases in the cells forming steroid hormones with these two groups of substrates gives absolutely different results which are presented in the table. These results are thought to be associated with presence of the isoenzyme, intensively splitting azotholphosphates, but inhibited by the diazonium salt. This isoenzyme is found mainly in the cells producing steroid hormones.
比较了在新生海豹的卵巢、睾丸和肾上腺、成年海豹的卵巢以及成年兔子、狗和人的肾上腺中形成类固醇激素的细胞中，使用不同底物检测磷酸酶的结果。第一组底物包括甘油磷酸钠、葡萄糖 -1- 磷酸、硝基苯磷酸酯（Gomori 硫化法）。第二组包括萘酚磷酸酯 AS - BI、AS - MX 和 AS - BS，其水解通过与重氮化联苯胺和稳定重氮酸盐同时及连续偶氮偶联，分别用坚牢蓝和坚牢樱桃红进行测定。用这两组底物检测形成类固醇激素的细胞中的磷酸单酯酶，得到的结果完全不同，如下表所示。这些结果被认为与一种同工酶的存在有关，该同工酶能强烈分解偶氮磷酸酯，但受重氮盐抑制。这种同工酶主要存在于产生类固醇激素的细胞中。
