Tributyltin sensitivity of vacuolar-type Na(+)-transporting ATPase from Enterococcus hirae.
Tributyltin sensitivity of vacuolar-type Na(+)-transporting ATPase from Enterococcus hirae.
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海拉肠球菌液泡型 Na() 转运 ATP 酶的三丁基锡敏感性。
DOI:
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发表时间:
2009
影响因子:
2
通讯作者:
Y. Kakinuma
中科院分区:
文献类型:
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作者:
Soracom Chardwiriyapreecha;Tomohiro Inoue;Naoko Sugimoto;T. Sekito;I. Yamato;T. Murata;M. Homma;Y. Kakinuma
Tributyltin chloride (TBT), an environmental pollutant, is toxic to a variety of eukaryotic and prokaryotic organisms. Some members of F-ATP synthase (F-ATPase)/vacuolar type ATPase (V-ATPase) superfamily have been identified as the molecular target of this compound. TBT inhibited the activities of H(+)-transporting or Na(+)-transporting F-ATPase as well as H(+)-transporting V-ATPase originated from various organisms. However, the sensitivity to TBT of Na(+)-transporting V-ATPase has not been investigated. We examined the effect of TBT on Na(+)-transporting V-ATPase from an eubacterium Enterococus hirae. The ATP hydrolytic activity of E. hirae V-ATPase in purified form as well as in membrane-bound form was little inhibited by less than 10 microM TBT; IC50 for TBT inhibition of purified enzyme was estimated to be about 35 microM. Active sodium transport by E. hirae cells, indicating the in vivo activity of this V-ATPase, was not inhibited by 20 microM TBT. By contrast, IC50 of H(+)-transporting V-ATPase of the vacuolar membrane vesicles from Saccharomyces cerevisiae was about 0.2 microM. E. hirae V-ATPase is thus extremely less sensitive to TBT.
DOI:
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发表时间:
1991
期刊:
The Journal of biological chemistry
影响因子:
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作者:
Powers,MF;Beavis,AD
通讯作者:
Beavis,AD