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- W2017145710 abstract "The enzymic and immunological properties of a novel γ-glutamyl transpeptidase found in human renal carcinoma tissues were investigated further in comparison with those of the normal kidney enzyme. On isoelectric focusing, the novel γ-glutamyl transpeptidase separated into two main forms, having p1 values below 3.6, while the normal kidney enzyme separated into multi-molecular forms with p1 values of 4.0–5.0. Neuraminidase treatment diminished the difference between these two enzymes, the products of the novel enzyme and the normal kidney having p1 values of 5.4 and 5.6, respectively. The percentages of the total activity of the novel γ-glutamyl transpeptidase binding with Con A before and after neuraminidase treatment were about 40% and 80%, respectively, while the corresponding percentages of the activity of the normal kidney enzyme were less than 10% and about 25%, respectively. The novel γ-glutamyl transpeptidase was immunologically identical with the normal kidney enzyme in the activity inhibition test and the double diffusion test. The present data suggest that the novel γ-glutamyi transpeptidase has the same antigen site as the normal kidney enzyme, but differs from the latter at least in its sialic acid content and in some other carbohydrate moieties." @default.
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- W2017145710 date "1981-05-01" @default.
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- W2017145710 title "Further investigations on a novel γ-glutamyl transpeptidase in human renal carcinoma" @default.
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- W2017145710 doi "https://doi.org/10.1016/0009-8981(81)90371-5" @default.
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