Open AccessNeomycin inhibition of adenosine triphosphatase: evidence for a neomycin-phospholipid interaction
Author(s) -
James J. Lipsky,
Paul S. Lietman
Publication year - 1980
Publication title -
antimicrobial agents and chemotherapy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.07
H-Index - 259
eISSN - 1070-6283
pISSN - 0066-4804
DOI - 10.1128/aac.18.4.532
Subject(s) - neomycin , triphosphatase , atpase , sodium , adenosine triphosphatase , phospholipid , biochemistry , chemistry , arrhenius plot , adenosine triphosphate , potassium , enzyme , biophysics , biology , membrane , activation energy , antibiotics , organic chemistry
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.