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Enzyme Research Unit, The South African Institute for Medical Research, Johannesburg, South Africa
The activities of pyruvate carboxylase (PC), phosphoenolpyruvate carboxykinase (PEPCK), glucose-6-phosphatase (G6Pase), and glycogen synthetase (GS) were determined in the cancerous and in the apparently uninvolved (host) regions of livers from primary hepatoma patients as well as in normal adult human livers and human fetal livers. The activities of these enzymes were also assayed in a fairly fast-growing, 3'-methyl-4-dimethylaminoazobenzene-induced transplantable rat hepatoma and in hepatoma cell lines derived from both rat and human tumors.
In the human hepatoma, as in the rat hepatoma, the activities of PC, PEPCK, and G6Pase were considerably reduced, compared to those in the host liver. The activities of both the a (glucose 6-phosphate-independent) and b (glucose 6-phosphate-dependent) forms of GS were also lower in human and rat hepatomas than in the respective host livers. Activities of PC, PEPCK, and G6Pase in the human hepatomas were often comparable with those of fetal livers. In rat and human hepatoma cells, the activities of PC, PEPCK, and G6Pase were similar to or lower than the activities in the respective hepatomas; the activities of GS a were also similar to those in the hepatoma, whereas the activities of GS b were somewhat higher.
1 This work was supported in part by grants from the Medical Research Council and the Atomic Energy Board of South Africa.
2 This study forms part of a thesis submitted for a Ph.D. degree to the University of the Witwatersrand, Johannesburg, South Africa. Present address: Department of Chemical Pathology, St. Mary's Hospital Medical School, London W. 2 1PG, England.
3 Present address: Department of Biochemistry and Biophysics, Iowa State University, Ames, Iowa 50011. To whom requests for reprints should be addressed.
Received 5/ 6/77. Accepted 2/10/78.
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