Felicetti D, Rath F W, Jänisch W
Acta Biol Med Ger. 1979;38(4):K13-K17.
A zinc activated tartrate resistent phosphatase (ZnTP) of the brain of different animal species was separated by electrofocusing in polyacrylamide gels. It is demonstrable selectively in the presence of 20 mM zinc acetate and 10 mM D,L-sodium tartrate or of 100 mM zinc acetate only. The ZnTP hydrolyzes 1-naphthyl phosphate and 4-nitrophenyl phosphate, respectively. High activity of ZnTP is evident in the brains of rats and rabbits. The activity is moderate or absent in the brains of mice, syrian-hamsters, sheeps, cats, rhesus monkeys, and of human beings. The isoelectric points of the enzyme from the various species are different, but the molecular weight is identical (65 000 estimated by gelfiltration on Sephadex G 100 in the brain of rat, rabbit, syrian-hamster, and man). A method of quantitative evaluation of ZnTP activity is described.
通过在聚丙烯酰胺凝胶中进行电聚焦，分离出不同动物物种大脑中的锌激活抗酒石酸磷酸酶（ZnTP）。只有在存在20 mM乙酸锌和10 mM D，L - 酒石酸钠或仅100 mM乙酸锌的情况下，才能选择性地证明其存在。ZnTP分别水解1 - 萘基磷酸酯和4 - 硝基苯基磷酸酯。ZnTP在大鼠和兔子的大脑中活性很高。在小鼠、叙利亚仓鼠、绵羊、猫、恒河猴和人类的大脑中，该活性中等或不存在。来自不同物种的该酶的等电点不同，但分子量相同（通过在大鼠、兔子、叙利亚仓鼠和人类大脑中在Sephadex G 100上进行凝胶过滤估计为65000）。描述了一种定量评估ZnTP活性的方法。
