Vanadate inhibition of Na+K+. ATPase and K+-dependent p-nitrophenylphosphatase: a kinetic analysis.

A Blázovics, L Vodnyánszky, J Somogyi, I Horváth
{"title":"Vanadate inhibition of Na+K+. ATPase and K+-dependent p-nitrophenylphosphatase: a kinetic analysis.","authors":"A Blázovics,&nbsp;L Vodnyánszky,&nbsp;J Somogyi,&nbsp;I Horváth","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Vanadate in redox state +5 inhibited the Na+K+-activated ATPase as well as the potassium-stimulated p-nitrophenylphosphatase (p-NPPase) activities of plasma membrane fragments prepared from rat brain. Vanadate exhibited a mixed type inhibition on the Na+K+-ATP-ase activity. The same type of inhibition was observed when the p-NPPase activity of the enzyme preparation was measured either in the presence of 20 mM K+ or with 5 mM Na+ + 1 mM K+. When the reaction mixture contained 50 microM ATP, 5 mM Na+ and 1 mM K+, inhibition of p-NPP hydrolised by vanadate displayed a noncompetitive character. Higher noradrenalin concentration was required for counteracting, the inhibition of p-NPPase by vanadate in the presence of ATP than in its absence.</p>","PeriodicalId":7308,"journal":{"name":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1983-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta biochimica et biophysica; Academiae Scientiarum Hungaricae","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

Vanadate in redox state +5 inhibited the Na+K+-activated ATPase as well as the potassium-stimulated p-nitrophenylphosphatase (p-NPPase) activities of plasma membrane fragments prepared from rat brain. Vanadate exhibited a mixed type inhibition on the Na+K+-ATP-ase activity. The same type of inhibition was observed when the p-NPPase activity of the enzyme preparation was measured either in the presence of 20 mM K+ or with 5 mM Na+ + 1 mM K+. When the reaction mixture contained 50 microM ATP, 5 mM Na+ and 1 mM K+, inhibition of p-NPP hydrolised by vanadate displayed a noncompetitive character. Higher noradrenalin concentration was required for counteracting, the inhibition of p-NPPase by vanadate in the presence of ATP than in its absence.

钒酸盐对Na+K+的抑制作用。atp酶和K+依赖性对硝基苯基磷酸酶:动力学分析。
氧化还原+5状态的钒酸盐抑制了Na+K+激活的atp酶和钾刺激的对硝基苯基磷酸酶(p-NPPase)活性。钒酸盐对Na+K+- atp酶活性有混合型抑制作用。当酶制剂在20 mM K+或5 mM Na+ + 1 mM K+存在下测量p-NPPase活性时,观察到相同类型的抑制。当反应混合物中含有50 μ m ATP、5 μ m Na+和1 μ m K+时,钒酸盐对p-NPP水解的抑制表现为非竞争性。钒酸盐对p-NPPase的抑制作用在ATP存在时比在ATP不存在时需要更高的去甲肾上腺素浓度。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信