人类孔蛋白的研究

Winkelbach H., Walter G., Moryswortmann C., Paetzold G., Hesse D., Zimmermann B., Florke H., Reymann S., Stadtmuller U., Thinnes F.P., Hilschmann N.
{"title":"人类孔蛋白的研究","authors":"Winkelbach H.,&nbsp;Walter G.,&nbsp;Moryswortmann C.,&nbsp;Paetzold G.,&nbsp;Hesse D.,&nbsp;Zimmermann B.,&nbsp;Florke H.,&nbsp;Reymann S.,&nbsp;Stadtmuller U.,&nbsp;Thinnes F.P.,&nbsp;Hilschmann N.","doi":"10.1006/bmmb.1994.1042","DOIUrl":null,"url":null,"abstract":"<div><p>Eight mouse monoclonal antibodies directed against the acetylated N-terminal part of the type 1 human VDAC Porin 31HL clearly discriminate type 1 and type 2 mammalian porin channels. This is shown by comparing synthetic N-terminal peptides of either channel type in Western dot blots or by ELISA. The data support the specificity of the anti-Porin 31HL antibodies and thus give further support to our recent observations on extramitochondrial expression of VDAC. In the plasmalemma of different mammalian cells VDAC forms part of an ubiquitous chloride channel complex, which in patch clamp measurements may figure as the outwardly rectifying depolarization-induced chloride channel that is affected in cystic fibrosis.</p></div>","PeriodicalId":8752,"journal":{"name":"Biochemical medicine and metabolic biology","volume":"52 2","pages":"Pages 120-127"},"PeriodicalIF":0.0000,"publicationDate":"1994-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/bmmb.1994.1042","citationCount":"52","resultStr":"{\"title\":\"Studies on Human Porin\",\"authors\":\"Winkelbach H.,&nbsp;Walter G.,&nbsp;Moryswortmann C.,&nbsp;Paetzold G.,&nbsp;Hesse D.,&nbsp;Zimmermann B.,&nbsp;Florke H.,&nbsp;Reymann S.,&nbsp;Stadtmuller U.,&nbsp;Thinnes F.P.,&nbsp;Hilschmann N.\",\"doi\":\"10.1006/bmmb.1994.1042\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Eight mouse monoclonal antibodies directed against the acetylated N-terminal part of the type 1 human VDAC Porin 31HL clearly discriminate type 1 and type 2 mammalian porin channels. This is shown by comparing synthetic N-terminal peptides of either channel type in Western dot blots or by ELISA. The data support the specificity of the anti-Porin 31HL antibodies and thus give further support to our recent observations on extramitochondrial expression of VDAC. In the plasmalemma of different mammalian cells VDAC forms part of an ubiquitous chloride channel complex, which in patch clamp measurements may figure as the outwardly rectifying depolarization-induced chloride channel that is affected in cystic fibrosis.</p></div>\",\"PeriodicalId\":8752,\"journal\":{\"name\":\"Biochemical medicine and metabolic biology\",\"volume\":\"52 2\",\"pages\":\"Pages 120-127\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1006/bmmb.1994.1042\",\"citationCount\":\"52\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemical medicine and metabolic biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0885450584710425\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemical medicine and metabolic biology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0885450584710425","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 52

摘要

针对1型人VDAC孔蛋白31HL乙酰化n端部分的8种小鼠单克隆抗体可明显区分1型和2型哺乳动物孔蛋白通道。这是通过比较两种通道类型的合成n端肽(Western dot blots或ELISA)来证明的。这些数据支持了抗porin 31HL抗体的特异性,从而进一步支持了我们最近对VDAC的线粒体外表达的观察。在不同哺乳动物细胞的质膜中,VDAC形成了无处不在的氯离子通道复合物的一部分,在膜片钳测量中,它可能被认为是囊性纤维化中受影响的向外整流去极化诱导的氯离子通道。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Studies on Human Porin

Eight mouse monoclonal antibodies directed against the acetylated N-terminal part of the type 1 human VDAC Porin 31HL clearly discriminate type 1 and type 2 mammalian porin channels. This is shown by comparing synthetic N-terminal peptides of either channel type in Western dot blots or by ELISA. The data support the specificity of the anti-Porin 31HL antibodies and thus give further support to our recent observations on extramitochondrial expression of VDAC. In the plasmalemma of different mammalian cells VDAC forms part of an ubiquitous chloride channel complex, which in patch clamp measurements may figure as the outwardly rectifying depolarization-induced chloride channel that is affected in cystic fibrosis.

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
期刊最新文献
Characteristics of Proteinuria in Experimental Diabetes Mellitus Time Dependence of Plasma Malondialdehyde, Oxypurines, and Nucleosides during Incomplete Cerebral Ischemia in the Rat ATP-Dependent Transport of Glutathione-N-Ethylmaleimide Conjugate across Erythrocyte Membrane Enzymatic and Secretory Activities in Pancreatic-Islets of Non-Insulin-Dependent Diabetic Rats after Short-Term Infusion of Succinic Acid Monomethyl Ester Rabbit Optic Nerve Phosphorylates Glucose through a Glucokinase-like Enzyme: Studies in Normal and Spontaneously Hyperglycemic Animals
×
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
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 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 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1