Enzymes of normal and malignant trophoblast: Phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase

In this study we compare the specific activities and isoenzyme patterns of five enzymes-phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase-in term placenta with the analogous enzymes in a clone of choriocarcinoma cells grown in culture. Phosphoglucose isomerase, phosphoglucomutase, and lactate dehydrogenase specific activities of the choriocarcinoma did not differ by more than two or three times from the mean activities of the comparable enzymes in placenta; the specific activity of hexokinase in the choriocarcinoma amounted to 14 per cent of the mean value for placenta. In contrast, the mean specific activity of heat-stable alkaline phosphatase in the choriocarcinoma amounted to only 1 per cent of the mean value for placenta. By growing the cells in 5-bromodeoxyuridine, 20 μg per milliliter, we were able to increase alkaline phosphatase activity to 68 per cent of the mean value for placenta. For both extracts, phosphoglucose isomerase zymograms were similar and phosphoglucomutase zymograms were similar. The hexokinase zymogram of term placenta showed two isoenzymes which stained more intensely with 0.5 mM. glucose than with 0.1M glucose. A hexokinase isoenzyme was observed in zymograms of both extracts which stained more intensely with 0.1M glucose than with 0.5 mM. glucose. Lactate dehydrogenase exhibited an extra isoenzyme in the choriocarcinoma extract. When the cells were cultivated in medium containing 5 μg per milliliter of 5-bromodeoxyuridine, the induced phosphatase in the cell line was electrophoretically similar to placental phosphatase. At higher concentrations of 5-bromodeoxyuridine, the most anodal isoenzyme was 0.5 cm. slower in mobility than the comparable placental isoenzyme.