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Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells.
Author(s) -
Emma Jean Bowman,
Annette Siebers,
Karlheinz Altendorf
Publication year - 1988
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.21.7972
Subject(s) - bafilomycin , atpase , vacuole , biochemistry , f atpase , biology , p type atpase , endoplasmic reticulum , bacteria , enzyme , cytoplasm , chloroplast , gene , autophagy , apoptosis , thylakoid , genetics
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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