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Last Updated: 2 years ago

Possible Interaction: Adenosine Triphosphate and Edetic Acid

Research Papers that Mention the Interaction

EDTA potentiated actions of ADP and ATP on endothelial cells by 2.4- and 3.6-fold, respectively.
Molecular pharmacology  •  1998  |  View Paper
Permeabilization induced by ATP was augmented by chelation of divalent cations with ethylene-diamine-tetraacetic acid and by the addition of lanthanum or cerium (0.01 to 1 mM).
The Journal of investigative dermatology  •  1993  |  View Paper
Presence of EDTA inhibited conversion of ADP to ATP (prior to luminescence measurement), presumably through a drop in pH caused by the interaction between H 2 EDTA 2− and the Mg 2+ of the pyruvate-kinase system employed.
Analytical biochemistry  •  1972  |  View Paper
The addition of ATP and Mg ++ together enhanced the inhibition of lactic acid production seen with ATP alone, as did the addition of ATP and EDTA together.
The Journal of laboratory and clinical medicine  •  1967  |  View Paper
The studies reported here demonstrate that ATP may be used in lieu of EDTA to inhibit nuclease digestion of DNA and chromatin.
Molecular and Cellular Biochemistry  •  2004  |  View Paper
The addition of EDTA to PPi and ATP exhibits more potent inactivation, even though EDTA alone does not inactivate phosphatase.
Molecular and Cellular Biochemistry  •  2004  |  View Paper
A 'stop solution' containing EDTA was prepared, which greatly retarded plasma ATP degradation by chelating Mg(+2) and Ca(+2) that are co-factors for many ATPases.
Luminescence : the journal of biological and chemical luminescence  •  2003  |  View Paper
The V-ATPase inhibitors, suramin, EGTA or EDTA significantly reduced the granular size increase in the presence of ATP.
Receptors & channels  •  1999  |  View Paper
This ecto‐ATPase activity was abolished in the presence of EDTA and was inhibited by 57±11% (n=3) by 200 μM αβ‐MeATP.
British journal of pharmacology  •  1998  |  View Paper
3 In the presence of EDTA (1 mm), the basal level of inositol trisphosphate (InsP3) was markedly increased and the absolute maximal response to ATP was decreased; however, the response to low concentrations of ATP was enhanced.
British journal of pharmacology  •  1993  |  View Paper
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