Podhajcer O L, Filmus J E, Mordoh J
Clin Chem. 1986 Feb;32(2):279-82.
Acid phosphatase (EC 3.1.3.2) isoenzyme 3 was purified from normal and malignant human mammary tissue and its properties in each were compared. The relative molecular mass of each was 53 000, as measured by sodium dodecyl sulfate gel electrophoresis. Several phosphomonoesters are good substrates for the isoenzymes, whereas organic and inorganic pyrophosphates and phosphoryl choline are hydrolyzed very slowly or not detectably. The optimum pH for interaction of these isoenzymes with p-nitrophenyl phosphate as substrate ranges from 3.5 to 4.5. L-(+)-Tartrate is a very strong inhibitor, Ki = 0.028 +/- 0.04 mmol/L (mean +/- SE), as are mercuric and fluoride ions in low concentrations. We conclude that type 3 isoenzymes obtained from normal and malignant tissue are very similar, though the malignant tissue appears to have a greater proportion of this type than does normal tissue.
酸性磷酸酶（EC 3.1.3.2）同工酶3从正常和恶性人乳腺组织中纯化出来，并比较了其在每种组织中的特性。通过十二烷基硫酸钠凝胶电泳测定，每种同工酶的相对分子质量为53000。几种磷酸单酯是这些同工酶的良好底物，而有机和无机焦磷酸以及磷酸胆碱的水解非常缓慢或无法检测到。这些同工酶与对硝基苯磷酸作为底物相互作用的最佳pH范围为3.5至4.5。L-(+)-酒石酸是一种非常强的抑制剂，Ki = 0.028 +/- 0.04 mmol/L（平均值 +/- 标准误），低浓度的汞离子和氟离子也是如此。我们得出结论，从正常和恶性组织中获得的3型同工酶非常相似，尽管恶性组织中这种类型的比例似乎比正常组织更高。
