巴非霉素
ATP酶
液泡
生物化学
F-ATP酶
生物
型三磷酸腺脢
内质网
细菌
酶
细胞质
叶绿体
细胞凋亡
遗传学
类囊体
自噬
基因
作者
Emma Jean Bowman,Annette Siebers,Karlheinz Altendorf
标识
DOI:10.1073/pnas.85.21.7972
摘要
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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