D-glyceraldehyde-3-phosphate dehydrogenase from HeLa cells--1. Purification and properties of the enzyme.
1. D-GPDH from HeLa cells was isolated and purified. 2. Some basic kinetic constants are reported. 3. Sodium dodecyl polyacrylamide gel electrophoresis gave a single band with a molecular weight of approximately 36 K. 4. ATP and NADH inhibit competitively enzyme activity. 5. Comparative catalytic properties of GPDH from normal and tumor cells were effectuated.
Nakano
M
M
Department of Biochemistry, University of Paraná, Curitiba, Brasil.
Funayama
S
S
de Oliveira
M B
MB
Bruel
S L
SL
Gomes
E M
EM
D001149:Arsenates / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability / Q000502:physiology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry / Q000187:drug effects / Q000302:isolation & purification*; D006019:Glycolysis / Q000502:physiology*; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D008954:Models, Biological; D009363:Neoplasm Proteins / Q000096:biosynthesis*; D010427:Pentose Phosphate Pathway / Q000502:physiology*; D012044:Regression Analysis
D001149:Arsenates; D009363:Neoplasm Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; C025657:arsenic acid