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PURIFICATION OF γ‐GLUTAMYLTRANSPEPTIDASE (γ‐GTP) FROM HUMAN HEPATOCELLULAR CARCINOMA (HCC), AND COMPARISON OF γ‐GTP WITH THE ENZYME FROM HUMAN KIDNEY a
Author(s) -
Toya Daishu,
Sawabu Norio,
Ozaki Kenji,
Wakabayashi Tokio,
Nakagen Masatoshi,
Hattori Nobu
Publication year - 1983
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1983.tb32852.x
Subject(s) - medicine
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.