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Last Updated: 3 years ago

Possible Interaction: Magnesium Chloride and Potassium Chloride

Research Papers that Mention the Interaction

Adding KCl in the presence of MgCl2 increased binding, with aK0.5 for KCl near 0.5 mM; the increased binding was associated with a drop inKd for vanadate to 11 nM but with no change in maximal binding.
Journal of bioenergetics and biomembranes  •  1981  |  View Paper
Increasing potassium chloride concentration from 0 to 100mM and magnesium chloride from 0 to 2mM show a parallel rate increase in polymerizing actin, whereas increasing calcium chloride concentration from 0 to 0.2mM decreases the rate of polymerizing actin.
Cell biology international  •  2002  |  View Paper
Pretreatment of the dentinal cavity with CaCl2, MgCl2 or SrCl2 greatly reduced the response of intradental nerves to KCl.
Archives of oral biology  •  1991  |  View Paper
Voltage-clamp experiments on single frog (Rana pipiens) atrial cells using whole cell recording techniques revealed that the addition of MgCl2 to the 150 mM KCl patch pipette solution influenced the voltage- and time-dependent potassium current (IK).
The American journal of physiology  •  1989  |  View Paper
Our results show that thick filaments dissociate from both ends on increasing the KCl concentration in the presence of 10 mM pyrophosphate and 5 mM MgCl2.
Biophysical journal  •  1985  |  View Paper
MgCl2 and spermine also interfered with the effect of KCl.
Biochimica et biophysica acta  •  1982  |  View Paper
The protein factor inhibited the rate and the extent of actin polymerization under nearly physiological conditions (for example, in 3 mM MgCl2 plus 90 mM KCl at pH 6.8).
Journal of biochemistry  •  1981  |  View Paper
KCl decreased AMP-PNP binding in the presence or absence of MgCl2 , but the simultaneous presence of a molar excess of NaCl abolished (or masked) the effect of KCl.
Journal of bioenergetics and biomembranes  •  1980  |  View Paper
Addition of KCl to the enzyme before the addition of ATP plus MgCl2 resulted in a low rate and extent of phosphorylation.
The Journal of biological chemistry  •  1979  |  View Paper
The RNAse eluted from CM-cellulose at 0.075 M KCl was almost completely inhibited by anti-RNAse A serum and by the endogenous RNAse inhibitor and a 33% inhibition was observed in the presence of 5 mM MgCl2.
Biochimica et biophysica acta  •  1976  |  View Paper
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