Matsumoto K, Kubota H, Kobayashi Y, Hayano K
Jikken Dobutsu. 1977 Jul;26(3):223-9. doi: 10.1538/expanim1957.26.3_223.
Biochemical properties of alkaline phosphatase (ALP) from placenta were compared between man, dog, cat, rabbit and cattle. 1) Optimum pH of the enzyme was essentially identical through the species of the animals but the inhibition of L-phenylalanine was clearly demonstrable with human ALP but little with that of other animals. 2) ALP of human placenta was not inactivated by heating at 65 degrees C for 15 min. but one of the other animals was thermolabile. Such thermostability of human placental ALP almost disappeared after treatment with EDTA, suggesting that the divalent metal ions were required for the thermostability. 3) Activities of placental ALP were inhibited by cationsurfactants in human and rat but not in the other animals, while the inhibition by DOC-Na, an anion-surfactant, was seen only in human. 4) The affinity to beta-glycerophosphae of placental ALP was seen only in human.
对人、犬、猫、兔和牛胎盘碱性磷酸酶（ALP）的生化特性进行了比较。1）该酶的最适pH值在不同动物物种间基本相同，但L-苯丙氨酸对人ALP有明显抑制作用，对其他动物的ALP抑制作用较小。2）人胎盘ALP在65℃加热15分钟不会失活，但其他动物的ALP对热不稳定。人胎盘ALP的这种热稳定性在用EDTA处理后几乎消失，表明二价金属离子是热稳定性所必需的。3）阳离子表面活性剂对人和大鼠胎盘ALP的活性有抑制作用，对其他动物则无，而阴离子表面活性剂十二烷基磺酸钠（DOC-Na）的抑制作用仅见于人。4）胎盘ALP对β-甘油磷酸的亲和力仅见于人。
