5-Phosphoribosyl pyrophosphate synthetase from Ehrlich ascites tumor cells

Biochemistry ◽  
1969 ◽  
Vol 8 (4) ◽  
pp. 1608-1614 ◽  
Author(s):  
P. C. L. Wong ◽  
Andrew W. Murray
1969 ◽  
Vol 47 (4) ◽  
pp. 419-422 ◽  
Author(s):  
Lydia J. Fontenelle ◽  
J. Frank Henderson

Incubation of tumor cells with formiminoglutamate leads to inhibition of lactate synthesis from glucose, inhibition of phosphoribosyl pyrophosphate synthesis, and inhibition of purine ribonucleotide synthesis de novo and from purine bases. Lactate synthesis from inosine was increased. These effects may result from inhibition of triose phosphate isomerase by a metabolite of formiminoglutamate.


1977 ◽  
Vol 55 (8) ◽  
pp. 834-840 ◽  
Author(s):  
Jerzy Barankiewicz ◽  
Mary L. Battell ◽  
J. Frank Henderson

Concentrations of intracellular orthophosphate were determined in Ehrlich ascites tumor cells incubated with glucose, inosine, or uridine in media of different orthophosphate concentration. The effects of orthophosphate concentration on the accumulation of lactate and of phosphoribosyl pyrophosphate and on concentrations of ribose 1-phosphate and ribose 5-phosphate in tumor cells incubated with glucose were also determined. Both the phosphorolysis of inosine and the rate of catabolism of ATP in cells incubated with 2-deoxyglucose were also influenced by the orthophosphate concentration of the medium.


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