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. 1980 Oct;18(4):532–535. doi: 10.1128/aac.18.4.532

Neomycin inhibition of adenosine triphosphatase: evidence for a neomycin-phospholipid interaction.

J J Lipsky, P S Lietman
PMCID: PMC284044  PMID: 6449904

Abstract

The inhibition of canine renal sodium potassium adenosine triphosphatase (ATPase) by neomycin was examined. Neomycin inhibited ATPase nearly maximally at 0.02 mM. The inhibition was temperature dependent with a decrease in inhibition occurring at temperatures below 21 degrees C, a temperature which corresponded to a change in activation energy of the ATPase as determined by Arrhenius plot. Preincubation of the ATPase with phosphoinositides was found to prevent the inhibition by neomycin. Other phospholipids were not found to prevent the inhibition. These results indicate a possible interaction between neomycin and the phosphoinositides of the ATPase complex.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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