Thallous ion activation of p-nitrophenylphosphatase of rat myometrium plasma membrane

1981 ◽  
Vol 59 (11) ◽  
pp. 1180-1183 ◽  
Author(s):  
A. K. Grover ◽  
M. Frederickson ◽  
E. E. Daniel

Addition of thallous ion (Tl+) inhibited the spontaneous mechanical activity of rat myometrium in K-free Krebs solution with an I50 value of 30 μM. The corresponding value for I50 for similar inhibition by addition of K+ was 150 μM. Tl+ as well as K+-activated p-nitrophenylphosphatase (PNPPase) of isolated rat myometrium plasma membrane vesicles. Half maximal activation was caused by 0.47 mM Tl+ or 1.6 mM K+. Maximal enzyme activities obtained using Tl+ and K+ were comparable. The Km values for the substrate p-nitrophenylphosphate using Tl+ (1.24 mM) and K+ (1.46 mM) were also similar. Activation by either ion was inhibited by ouabain, Na+, inorganic phosphate, and vanadate (V + 5). The results suggest that Tl+ can substitute for K+ for activation of the Na–K pump of rat myometrium plasma membrane.

1980 ◽  
Vol 58 (10) ◽  
pp. 1247-1250 ◽  
Author(s):  
A. K. Grover ◽  
T. R. Jones ◽  
E. E. Daniel

Vanadate inhibited K+-activated and K+-activated ouabain-sensitive p-nitrophenyl phosphatases of rat myometrium at nanomolar concentrations. The vanadate concentrations required for 50% inhibition were 220 ± 30 nM for the K+-activated component of this enzyme and 200 ± 30 nM for the K+-activated ouabain-sensitive component. Micromolar concentrations of vanadate inhibited acid and alkaline p-nitrophenyl phosphatases. ATP-dependent Ca uptake by the plasma membrane vesicles was not inhibited by 10 nM – 1 mM vanadate. Mg2+-ATPase was also not affected. Thus K+-activated and K+-activated ouabain-sensitive p-nitrophenyl phosphatase activities of the plasma membrane were most sensitive to inhibition by vanadate. Preliminary experiments demonstrated that similar to ouabain, vanadate inhibited potassium-induced abolition of spontaneous contractile activity of isolated rat myometrium in K-free Krebs. This effect of vanadate is consistent with vanadate inhibition of K+-activated ouabain-sensitive p-nitrophenyl phosphatase.


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