PURIFICATION OF γ‐GLUTAMYLTRANSPEPTIDASE (γ‐GTP) FROM HUMAN HEPATOCELLULAR CARCINOMA (HCC), AND COMPARISON OF γ‐GTP WITH THE ENZYME FROM HUMAN KIDNEY a
PURIFICATION OF γ‐GLUTAMYLTRANSPEPTIDASE (γ‐GTP) FROM HUMAN HEPATOCELLULAR CARCINOMA (HCC), AND COMPARISON OF γ‐GTP WITH THE ENZYME FROM HUMAN KIDNEY a
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从人肝癌 (HCC) 中纯化 γ-谷氨酰转肽酶 (γ-GTP)，以及 γ-GTP 与人肾酶的比较
DOI：
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发表时间：
1983
期刊：
影响因子：
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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
为了阐明我们以前报道的肝癌血清特异性的新γ-GTP的特性，从肝癌组织中纯化γ-GTP，并将其理化和免疫学性质与正常成人肾酶进行比较。发现来自HCC组织和来自正常肾脏的酶在底物的Km值、最适pH、热稳定性、作为受体的各种氨基酸的作用、对阳离子或乙二胺四乙酸的行为以及免疫学性质方面相似或相同。然而，HCC组织酶与正常肾酶在分子量、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是可区分的。这些结果支持了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的设想。
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.