d-Glyceraldehyde-3-phosphate dehydrogenase from HeLa cells—1. Purification and properties of the enzyme

Abstract 1. 1. d -GDPH from HeLa cells was isolated and purified. 2. 2. Some basic kinetic constants are reported. 3. 3. Sodium dodecyl polyacrylamide gel electrophoresis gave a single band with a molecular weight of approximately 36 K. 4. 4. ATP and NADH inhibit competitively enzyme activity. 5. 5. Comparative catalytic properties of GPDH from normal and tumor cells were effectuated.