Back to Search
Start Over
Activities of some enzymes concerned with citrate and glucose metabolism in transplanted rat hepatomas.
- Source :
-
The Biochemical journal [Biochem J] 1966 Mar; Vol. 98 (3), pp. 874-82. - Publication Year :
- 1966
-
Abstract
- 1. Certain enzymes concerned with citrate and glucose metabolism have been measured in two transplanted rat hepatomas, one induced with ethionine (minimal deviation type) and one induced with dimethylaminoazobenzene. In these hepatomas both citrate-cleavage enzyme and NADP-linked isocitrate dehydrogenase in the soluble fraction of the cell were approximately one-third of the values for normal rat liver. These changes have been discussed in relation to the increased citric acid content of tumours and depressed rate of fatty acid synthesis. 2. The glucose-ATP-phosphotransferase activity was below normal liver values in the ethionine-induced tumour but greater than normal in the dimethylaminoazobenzene-induced hepatoma. The apparent K(m) values for the glucose-ATP phosphotransferases of these hepatomas were approx. 8x10(-5)m; no evidence was found for an enzyme with a high K(m) for glucose equivalent to liver glucokinase. 3. Of the enzymes of the pentose phosphate pathway, glucose 6-phosphate-dehydrogenase activity was three to five times as great whereas 6-phosphogluconate-dehydrogenase activity was the same or lower than normal liver in the ethionine-and dimethylaminoazobenzene-induced tumours respectively.
- Subjects :
- Animals
Carcinoma, Hepatocellular chemically induced
Ethionine pharmacology
In Vitro Techniques
Kinetics
Liver Neoplasms
Neoplasm Transplantation
Neoplasms, Experimental metabolism
Rats
p-Dimethylaminoazobenzene pharmacology
Carcinoma, Hepatocellular metabolism
Citrates metabolism
Glucokinase metabolism
Glucose metabolism
Glucosephosphate Dehydrogenase metabolism
Hexokinase metabolism
Isocitrate Dehydrogenase metabolism
Lyases metabolism
Phosphogluconate Dehydrogenase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0264-6021
- Volume :
- 98
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 4287845
- Full Text :
- https://doi.org/10.1042/bj0980874