Toya D, Sawabu N, Ozaki K, Wakabayashi T, Nakagen M, Hattori N
Ann N Y Acad Sci. 1983;417:86-96. doi: 10.1111/j.1749-6632.1983.tb32852.x.
In order to elucidate the characteristics of novel gamma-GTP, which was reported in our previous publications to be specific to sera of HCC, gamma-GTP was purified from HCC tissues, and its physicochemical and immunologic properties were compared with those of the normal adult kidney enzyme. The enzyme from HCC tissue and from normal kidney were found to be similar or identical with respect to the Km value for substrate, optimal pH, thermostability, effect of various amino acids as acceptors, behavior to cations or ethylendiaminetetraacetate, and immunologic properties. However, the HCC tissue enzyme was distinguishable from the normal kidney enzyme with respect to molecular weight, electrophoretic mobility before and after neuraminidase treatment, Con-A-affinity, sensitivity to neuraminidase, and isoelectrophoretic point. These results support the conceivability that novel gamma-GTP in the sera of HCC patients is largely due to structural differences in the carbohydrate moieties.
为了阐明我们之前的出版物中报道的肝癌患者血清特异性新型γ-谷氨酰转肽酶（γ-GTP）的特征，从肝癌组织中纯化γ-GTP，并将其理化性质和免疫特性与正常成人肾脏酶进行比较。发现肝癌组织和正常肾脏中的酶在底物Km值、最适pH值、热稳定性、各种氨基酸作为受体的作用、对阳离子或乙二胺四乙酸的反应以及免疫特性方面相似或相同。然而，肝癌组织酶在分子量、神经氨酸酶处理前后的电泳迁移率、刀豆球蛋白A亲和力、对神经氨酸酶的敏感性和等电点方面与正常肾脏酶不同。这些结果支持了这样一种设想，即肝癌患者血清中的新型γ-GTP很大程度上是由于碳水化合物部分的结构差异。
