Jeevaratnam et al., Toxicol Appl Pharmacol 1992
:
MIC also stimulated the ATPase activity in tightly coupled mitochondria while lipid peroxidation remained unaffected
Jeevaratnam et al., Arch Environ Contam Toxicol 1992
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MIC inhibited both acetylcholinesterase (AChE) and adenosine triphosphatase (ATPase) activities of erythrocytes dose-dependently in vitro, while in vivo a decreased trend in ATPase activity with unaltered AChE activity was observed
Jeevaratnam et al., Arch Toxicol 1995
:
Activation of Na+, K ( + ) -ATPase by ATP in the presence of MIC showed a decrease in Vmax with no change in Km. Similarly, activation of K+ PNPPase by PNPP in the presence of MIC showed a decrease in Vmax with no change in Km. The circular dichroism spectral studies revealed that MIC interaction with Na+, K ( + ) -ATPase led to a conformation of the protein wherein the substrates Na+ and K+ were no longer able to bind at the Na ( + ) - and K ( + ) -activation sites