Purification of gamma-glutamyltranspeptidase (gamma-GTP) from human hepatocellular carcinoma (HCC), and comparison of gamma-GTP with the enzyme from human kidney.
Purification of gamma-glutamyltranspeptidase (gamma-GTP) from human hepatocellular carcinoma (HCC), and comparison of gamma-GTP with the enzyme from human kidney.
复制标题
从人肝细胞癌 (HCC) 中纯化 γ-谷氨酰转肽酶 (gamma-GTP)，并将 γ-GTP 与人肾酶进行比较。
DOI：
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发表时间：
1983
影响因子：
5.2
通讯作者：
N. Hattori
中科院分区：
文献类型：
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作者：
D. Toya;N. Sawabu;K. Ozaki;T. Wakabayashi;M. Nakagen;N. Hattori
为了阐明我们之前的出版物中报道的 HCC 血清特异性的新型 γ-GTP 的特征，从 HCC 组织中纯化了 γ-GTP，并将其理化和免疫学特性与正常成人肾酶的特性进行了比较。发现来自 HCC 组织和来自正常肾脏的酶在底物 Km 值、最佳 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行为以及免疫学特性方面相似或相同。然而，HCC组织酶在分子量、神经氨酸酶处理前后的电泳迁移率、Con-A亲和力、对神经氨酸酶的敏感性和等电泳点方面与正常肾酶不同。这些结果支持这样的设想：HCC 患者血清中的新型 γ-GTP 主要是由于碳水化合物部分的结构差异。
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.