Abstract
Destruxin B, a peptide antibiotic, inhibits vacuolar-type ATPase (V-ATPase) specifically and dose-dependently among ATPases examined. Acidification of intracellular organelles is also blocked by destruxin B at comparable concentrations when assessed by accumulation of acridine orange. The inhibitory activity of destruxin B is weaker than that of bafilomycin A 1 and folimycin, well known macrolide inhibitors of V-ATPase, when compared at the same molar concentration. Unlike the macrolide antibiotics, however, the inhibitory activity of destruxin B is readily reversible. This novel feature of destruxin B should make it a useful probe in the analysis of V-ATPase function in cell physiology.
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