Szewczuk A, Milnerowicz H, Prusak E, Albert Z
Folia Histochem Cytochem (Krakow). 1982;20(1-2):25-33.
Using solubilization with bromelain, the light form of gamma-glutamyltransferase was purified from Morris hepatoma 5123D. Some properties of this enzyme were compared to those of the light form rat kidney GGT. Anthglutin and its isomer inhibit competitively the former enzyme but non-competitively the latter. On zymograms of rat control sera, five GGT fractions were noted, but in sera of rats with hepatoma 5123D also the light form and the increase of GGT activity ain region of fraction II were observed. Only these two enzyme fractions react with antibody anti heavy form of Morris hepatoma GGT.
利用菠萝蛋白酶增溶法，从莫里斯肝癌5123D中纯化出γ-谷氨酰转移酶的轻链形式。将该酶的一些特性与大鼠肾脏γ-谷氨酰转移酶轻链形式的特性进行了比较。蒽黄酮及其异构体对前一种酶有竞争性抑制作用，对后一种酶有非竞争性抑制作用。在大鼠对照血清的酶谱图上，发现有五个γ-谷氨酰转移酶组分，但在患5123D肝癌大鼠的血清中，也观察到了轻链形式以及组分II区域内γ-谷氨酰转移酶活性的增加。只有这两个酶组分与抗莫里斯肝癌γ-谷氨酰转移酶重链形式的抗体发生反应。
