Kinetics of the Mechanism of Action of Monoamine Oxidase in the Regulation of Na+, K+‐ATPase Activity in Rat Brain

C. S K Mayanil, N. Z. Baquer*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Kinetic studies on the action of monoamine oxidase (MAO) in the regulation of Na+,K+‐ATPase were performed using 3‐methoxy‐4‐hydroxybenzaldehyde (MHB), which is an analogue of 3‐methoxy‐4‐hydroxyphenylacetylaldehyde (product of MAO‐catalysed reaction with dopamine as substrate). It was observed that at 2.6 μM MHB, the activation of Na+,K+‐ATPase may be the result of the removal of the inhibitory Ca2+, thereby increasing the Vmax. Double‐reciprocal plots of Pi versus MHB showed that Ca2+ counteracted the effect of the aldehyde not by changing the Km, but be decreasing the Vmax of the Na+,K+‐ATPase stimulation. The removal of 3′,5′‐cyclic AMP‐dependent protein kinase from the microsomes by sodium dodecyl sulphate treatment abolished the activation and/or inhibition of the Na+,K+‐ATPase by aldehyde; it can therefore be inferred that 3′,5′‐cyclic AMP‐dependent protein kinase is involved in the regulation of Na+,K+‐ATPase.

Original languageEnglish (US)
Pages (from-to)25-30
Number of pages6
JournalJournal of Neurochemistry
Issue number1
StatePublished - Jan 1 1985


  • 3′,5′‐Cyclic AMP‐dependent protein kinase
  • Biogenie aldehyde
  • Dopamine
  • Microsomes
  • Monoamine oxidase
  • Na,K‐ATPase

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience


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