瓜质膜囊泡中NADH氧化酶的洗涤活性。

Letizia De Luca , Ursula Bader , Rainer Hertel , Paolo Pupillo
{"title":"瓜质膜囊泡中NADH氧化酶的洗涤活性。","authors":"Letizia De Luca ,&nbsp;Ursula Bader ,&nbsp;Rainer Hertel ,&nbsp;Paolo Pupillo","doi":"10.1016/0304-4211(84)90241-4","DOIUrl":null,"url":null,"abstract":"<div><p>In microsomes from <em>Cucurbita</em> hypocotyls a duroquinone (DQ) stimulated NADH oxidase was found which is strongly activated by addition of 0.01–0.1% Triton X-100. After density gradient centrifugation and polyethyleneglycol (PEG) fractionation this enzyme occurs in membranes carrying plasma membrane markers. Another NADH oxidase localized at the endoplasmic reticulum (e.r.) is not activated but inhibited by Triton. The data are consistent with closed and outside-out plasma membrane vesicles where the NADH site becomes accessible only after detergent permeabilization. A role of the enzyme in transmembrane transport of electrons and/or protons is discussed.</p></div>","PeriodicalId":20221,"journal":{"name":"Plant Science Letters","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1984-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0304-4211(84)90241-4","citationCount":"21","resultStr":"{\"title\":\"Detergent activity of NADH oxidase in vesicles derived from the plasmamembrane of Cucurbita pepo L.\",\"authors\":\"Letizia De Luca ,&nbsp;Ursula Bader ,&nbsp;Rainer Hertel ,&nbsp;Paolo Pupillo\",\"doi\":\"10.1016/0304-4211(84)90241-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>In microsomes from <em>Cucurbita</em> hypocotyls a duroquinone (DQ) stimulated NADH oxidase was found which is strongly activated by addition of 0.01–0.1% Triton X-100. After density gradient centrifugation and polyethyleneglycol (PEG) fractionation this enzyme occurs in membranes carrying plasma membrane markers. Another NADH oxidase localized at the endoplasmic reticulum (e.r.) is not activated but inhibited by Triton. The data are consistent with closed and outside-out plasma membrane vesicles where the NADH site becomes accessible only after detergent permeabilization. A role of the enzyme in transmembrane transport of electrons and/or protons is discussed.</p></div>\",\"PeriodicalId\":20221,\"journal\":{\"name\":\"Plant Science Letters\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1984-09-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0304-4211(84)90241-4\",\"citationCount\":\"21\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Plant Science Letters\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0304421184902414\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Plant Science Letters","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0304421184902414","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 21

摘要

在葫芦下胚轴微粒体中发现了duroquinone (DQ)刺激的NADH氧化酶,该酶在添加0.01 ~ 0.1% Triton X-100后被强烈激活。在密度梯度离心和聚乙二醇(PEG)分离后,这种酶发生在携带质膜标记物的膜上。另一种位于内质网(e.r)的NADH氧化酶不被激活,而是被Triton抑制。这些数据与封闭和由外向外的质膜囊一致,其中NADH位点只有在洗涤剂渗透后才能进入。讨论了酶在电子和/或质子跨膜传递中的作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Detergent activity of NADH oxidase in vesicles derived from the plasmamembrane of Cucurbita pepo L.

In microsomes from Cucurbita hypocotyls a duroquinone (DQ) stimulated NADH oxidase was found which is strongly activated by addition of 0.01–0.1% Triton X-100. After density gradient centrifugation and polyethyleneglycol (PEG) fractionation this enzyme occurs in membranes carrying plasma membrane markers. Another NADH oxidase localized at the endoplasmic reticulum (e.r.) is not activated but inhibited by Triton. The data are consistent with closed and outside-out plasma membrane vesicles where the NADH site becomes accessible only after detergent permeabilization. A role of the enzyme in transmembrane transport of electrons and/or protons is discussed.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
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