Szewczuk A, Milnerowicz H, Sobiech K A
Arch Immunol Ther Exp (Warsz). 1977;25(4):589-600.
Use of a four-step method of purification from human kidneys yielded gamma-glutamyl transpeptidase with specific activity 330 times higher than activity in the homogenate. The enzyme from human liver was also purified, and from urine two fractions of it were separated. From rabbits immunized with the enzyme from human kidney, antiserum was obtained which inhibits and precipitates the human-derived enzyme, and in a low degree the enzyme purified from bovine kidneys. This inhibition was independent of incubation time and precipitate formation, but dependent on the amount of antiserum used. A gamma-glutamyl transpeptidase complex with antibody was isolated on a column with CM-cellulose with electrophoretic mobility different from that of the native enzyme.
采用从人肾中进行四步纯化的方法，得到了γ-谷氨酰转肽酶，其比活性比匀浆中的活性高330倍。人肝中的该酶也得到了纯化，并且从尿液中分离出了它的两个组分。用来自人肾的酶免疫兔子，获得了抗血清，该抗血清能抑制并沉淀人源酶，对从牛肾中纯化的酶也有较低程度的抑制作用。这种抑制作用与孵育时间和沉淀形成无关，但取决于所用抗血清的量。在CM-纤维素柱上分离出了一种与抗体结合的γ-谷氨酰转肽酶复合物，其电泳迁移率与天然酶不同。
