Further investigations on the p-nitrophenylphosphatase activity of intact Ehrlich ascites tumor cells.
The substrate specificity and the effects of nucleotides and SH-blocking agents on the p-nitrophenylphosphatase activity of intact Ehrlich ascites tumor cells (EAT) cells were studied. DL-beta-Glycerophosphate, o-phosphoethanolamine, cholinephosphate, glucose-6-phosphate, o-carboxyphenylphosphate,, phosphoenolpyruvate and AMP were not attacked by intact cells. ATP is greater than GTP is greater than UPT is greater than PPi is greater than pNPP were cleaved with decreasing velocity. A stimulation of the cleavage of p-NPP by the following nucleotides was observed with decreasing effectivity: ATP is greater than ADP is greater than GTP is greater than UTP; AMP was ineffective. The phosphatase activity was not affected by malate, tartrate and glutathion disulfide. The SH blocking agents diamide and thimerosal were more effective inhibitors of the pNPPase than of the ATPase activity, whereas the hydrolysis of ATP is more affected by the ATP analog adenylylimidodiphosphate. The present data are best compatible with a double headed enzyme: Both active sites interact with ATP, only one is active against p-NPP and sensitive against SH-blocking agents.
D009597:4-Nitrophenylphosphatase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D004789:Enzyme Activation; D005260:Female; D051379:Mice; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D013379:Substrate Specificity
D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase