Studies on membrane ATPase activity and lipid level in vibrio el tor under normal and nitrofurantoin resistant conditions.
Nitrofurantoin resistance brought about decreased level of membrane bound ATPase activity in Vibrio el tor as compared to the normal strain while phospholipid as well as total lipid levels in the membrane fraction was increased. Mg++ was found to be the mose effective co-factor for ATPase. At higher concentrations of sodium and potassium ions, ATPase of normal and nitrofurantoin resistant Vibrio el tor responded quite differently. A soluble ATPase extract having low phospholipid content was found to be activated by the phospholipid extracts of Vibrio el tor, phosphatidyl ethanolamine, and also by phosphatidyl choline which is not a constituent of the membrane preparation of Vibrio el tor strains.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D002412:Cations / Q000494:pharmacology; D002462:Cell Membrane / Q000201:enzymology; D004352:Drug Resistance, Microbial; D008563:Membrane Lipids / Q000032:analysis*; D009582:Nitrofurantoin / Q000494:pharmacology*; D010743:Phospholipids / Q000032:analysis* / Q000494:pharmacology; D014733:Vibrio / Q000032:analysis* / Q000187:drug effects / Q000201:enzymology
D002412:Cations; D008563:Membrane Lipids; D010743:Phospholipids; D009582:Nitrofurantoin; D000251:Adenosine Triphosphatases