scholarly journals Synthesis, Characterization and Anti-Angiogenic Effects of Novel 5-Amino Pyrazole Derivatives on Ehrlich Ascites Tumor [EAT] Cells in-Vivo

2010 ◽  
Vol 01 (01) ◽  
pp. 1-9 ◽  
Author(s):  
H. Raju ◽  
S. Chandrappa ◽  
M. K. Ramakrishna ◽  
T. S. Nagamani ◽  
H. Ananda ◽  
...  
Keyword(s):  
Ehrlich Ascites Tumor ◽  
Pyrazole Derivatives ◽  
Ascites Tumor ◽  
Ehrlich Ascites ◽  
Eat Cells

N-Substituted-2-butyl-5-chloro-3H-imidazole-4-carbaldehyde Derivatives as Anti-tumor Agents Against Ehrlich Ascites tumor Cells In Vivo

2007 ◽  
Vol 3 (3) ◽  
pp. 269-276 ◽  
Author(s):  
C. Anil Kumar ◽  
S. Nanjunda Swamy ◽  
S. L. Gaonkar ◽  
Basappa ◽  
Bharathi P. Salimath ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Ehrlich Ascites

Further Investigations on the p-Nitrophenylphosphatase Activity of Intact Ehrlich Ascites Tumor Cells

1978 ◽  
Vol 33 (3-4) ◽  
pp. 227-230 ◽  
Author(s):  
Reiner Merz ◽  
Monika Löffler ◽  
Friedhelm Schneider
Keyword(s):  
Tumor Cells ◽  
Active Sites ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Intact Cells ◽  
Blocking Agents ◽  
Ehrlich Ascites ◽  
Eat Cells ◽  
Hydrolysis Of

The substrate specificity and the effects of nucleotides and SH-blocking agents on the p-nitro- phenylphosphatase activity of intact Ehrlich ascites tumor cells (EAT) cells were studied, ᴅʟ-β- Glycerophosphate, o-phosphoethanolamine, cholinephosphate, glucose-6-phosphate, o-carboxyphenyl- phosphate,, phosphoenolpyruvate and AMP were not attacked by intact cells. ATP > GTP > UTP > PPi > pNPP were cleaved with decreasing velocity. A stimulation of the cleavage of p-NPP by the following nucleotides was observed with decreasing effectivity: ATP > ADP > GTP > 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.

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