دورية أكاديمية
Quinacrine mustard and lipophilic cations inhibitory to both vacuolar H(+)-ATPase and F0F1-ATP synthase.
| العنوان: | Quinacrine mustard and lipophilic cations inhibitory to both vacuolar H(+)-ATPase and F0F1-ATP synthase. |
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| المؤلفون: | Moriyama Y; Department of Biochemistry and Organic Chemistry, Osaka University, Japan., Patel V, Futai M |
| المصدر: | FEBS letters [FEBS Lett] 1995 Feb 06; Vol. 359 (1), pp. 69-72. |
| نوع المنشور: | Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: John Wiley & Sons Ltd Country of Publication: England NLM ID: 0155157 Publication Model: Print Cited Medium: Print ISSN: 0014-5793 (Print) Linking ISSN: 00145793 NLM ISO Abbreviation: FEBS Lett Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Jan. 2016- : West Sussex : John Wiley & Sons Ltd. Original Publication: Amsterdam, North-Holland on behalf of the Federation of European Biochemical Societies. |
| مواضيع طبية MeSH: | Dequalinium/*pharmacology , Proton-Translocating ATPases/*antagonists & inhibitors , Quinacrine Mustard/*pharmacology , Vacuoles/*enzymology, Amino Acid Sequence ; Animals ; Binding, Competitive ; Brain/enzymology ; Cations ; Cattle ; Chlorpromazine/pharmacology ; Chromaffin Granules/enzymology ; Dithiothreitol/pharmacology ; Escherichia coli/enzymology ; Molecular Sequence Data ; Plants/enzymology ; Plants/ultrastructure ; Proton-Translocating ATPases/metabolism ; Quinacrine ; Quinacrine Mustard/metabolism ; Rats ; Synaptic Vesicles/enzymology |
| مستخلص: | Various lipophilic cations, such as quinacrine mustard and dequalinium, which are known to inhibit mitochondrial F1-ATPase, strongly inhibited vacuolar H(+)-ATPase purified from bovine adrenal chromaffin granules. Quinacrine mustard bound irreversibly to vacuolar H(+)-ATPase subunit A, and the 115 kDa accessory polypeptide and dithiothreitol had no effect. The binding was competitively inhibited by chlorpromazine and quinacrine, and these compounds specifically reduced the amount of labeling of subunit A. Quinacrine mustard also prevented the binding of [alpha-32P]ATP to subunit A but had no effect on the binding of [3H]N-ethylmaleimide to either subunit A or the 115 kDa accessory polypeptide. These results suggest that the binding site of quinacrine mustard in subunit A is not related to the N-ethylmaleimide-binding site(s), which is important for activity. |
| المشرفين على المادة: | 0 (Cations) 4213-45-0 (Quinacrine Mustard) E7QC7V26B8 (Dequalinium) EC 3.6.3.14 (Proton-Translocating ATPases) H0C805XYDE (Quinacrine) T8ID5YZU6Y (Dithiothreitol) U42B7VYA4P (Chlorpromazine) |
| تواريخ الأحداث: | Date Created: 19950206 Date Completed: 19950313 Latest Revision: 20190621 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1016/0014-5793(95)00013-y |
| PMID: | 7851533 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0014-5793 |
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| DOI: | 10.1016/0014-5793(95)00013-y |