Proceedings of the National Academy of Sciences · 1988 · 1.8K citations · 34 references
Life SciencesBiochemistryMicrobiologyBacteriologyEnzymologyMembrane BiochemistryEnzyme InhibitionMitochondrial MembranesCalcium AtpaseEscherichia ColiInhibitor SpecificityMembrane AtpasesNa-k-atpase ActivitySarcoplasmic Reticulum Calcium AtpasesSodium-potassium Adenosine TriphosphataseSodium-potassium Atpase
The study tested various membrane ATPases for sensitivity to the macrolide antibiotic bafilomycin A1. Bafilomycin A1 does not affect bacterial or mitochondrial F1F0 ATPases, moderately inhibits E1E2 ATPases such as bacterial Kdp, brain Na⁺/K⁺, and sarcoplasmic reticulum Ca²⁺ pumps, but potently blocks vacuolar ATPases from Neurospora, chromaffin granules, and plants, making it a valuable tool to differentiate ATPase classes.
Various membrane ATPases have been tested for their sensitivity to bafilomycin A1, a macrolide antibiotic. F1F0 ATPases from bacteria and mitochondria are not affected by this antibiotic. In contrast, E1E2 ATPases--e.g., the K+-dependent (Kdp) ATPase from Escherichia coli, the Na+,K+-ATPase from ox brain, and the Ca2+-ATPase from sarcoplasmic reticulum--are moderately sensitive to this inhibitor. Finally, membrane ATPases from Neurospora vacuoles, chromaffin granules, and plant vacuoles are extremely sensitive. From this we conclude that bafilomycin A1 is a valuable tool for distinguishing among the three different types of ATPases and represents the first relatively specific potent inhibitor of vacuolar ATPases.
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Peter Leth Jørgensen · Biochimica et Biophysica Acta (BBA) - Biomembranes · 1974 · 947 citations
Gerhard Werner, Hanspaul Hagenmaier, Hannelore Drautz et al. · The Journal of Antibiotics · 1984 · 330 citations · Full text