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., Walter G., Moryswortmann C., Paetzold G., Hesse D., Zimmermann B., Florke H., Reymann S., Stadtmuller U., Thinnes F.P., 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., Walter G., Moryswortmann C., Paetzold G., Hesse D., Zimmermann B., Florke H., Reymann S., Stadtmuller U., Thinnes F.P., 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}
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.