Papaveroline

Papaveroline inhibits rat brain microsomal Na⁺,K⁺-ATPase with an IC₅₀ of 0.20 mM and inhibits rat brain microsomal Mg²⁺-ATPase with an I₅₀ of 0.40 mM^[2].
Papaveroline inhibits rat brain microsomal K⁺-activated pNPPase with an IC₅₀ of 1.51 mM, which is less potent than its inhibition of rat brain microsomal Na⁺,K⁺-ATPase^[2].
Papaveroline (75-100% inhibition; 10 min)-mediated inhibition of rat brain microsomal Na⁺,K⁺-ATPase is freely reversible, as enzyme activity returns to control levels following washing and resuspension of the enzyme^[2].
Papaveroline (200-400 μM) acts as a simple linear noncompetitive inhibitor of rat brain microsomal Na⁺,K⁺-ATPase with respect to ATP, exhibiting an apparent K_i of 380.00 μM^[2].
Papaveroline (300 μM) decreases the apparent affinity of rat brain microsomal Na⁺,K⁺-ATPase for Na⁺ by increasing the K_0.5 by 65% without altering cooperative binding at the Na⁺ site or the enzyme's V_max^[2].
Papaveroline inhibits beef cardiac Na⁺,K⁺-ATPase with an IC₅₀ of 0.76 mM, which is less potent than its inhibition of rat brain microsomal Na⁺,K⁺-ATPase^[2].
Papaveroline (100-500 μM; 18 h) induces apoptosis in the majority of human dopaminergic neuroblastoma SH-SY5Y cells at 100 μM and 250 μM (69.19% and 83.07% apoptotic cells, respectively) and shifts to mostly necrosis at 500 μM (67.88% necrotic cells)^[3].
Papaveroline (250 μM; 3 h) does not significantly reduce intracellular ATP levels in human dopaminergic neuroblastoma SH-SY5Y cells, with a measured concentration of 4.79 nmol/mg protein after 3 h incubation^[3].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.