{"title":"Endogenous incorporation of 32 P in Neisseria meningitidis. I. The effects of CO2 and electron flux.","authors":"S. Jyssum, K. Jyssum","doi":"10.1111/J.1699-0463.1970.TB04312.X","DOIUrl":null,"url":null,"abstract":"Meningococcal extracts mediate an incorporation of 32P in the presence of Mg44 and ADP which is improved by the addition of EDTA. A major part of this incorporation is due to a polynucleotide phosphorylase activity, and is independent of electron flux. But the endogenous respiration is also accompanied by a phosphorylation. When the cytochrome oxidase is inhibited by KCN phosphorylation occurs concomitantly with the endogenous reduction of added mammalian ferricytochrome c. This phosphorylation is nearly doubled when KHCO3 is included in the system. It has not been possible to demonstrate an oxidative phosphorylation on the electron-oxygen transport level in meningococcal extracts with NADH, NADPH or ferrocytochrome c as electron sources. The phosphorylation connected with electron flux, and its enhancement by KHCO3 have been discussed in relation to the CO2 requirements typical for N. meningitidis.","PeriodicalId":7323,"journal":{"name":"Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology","volume":"61 1","pages":"337-42"},"PeriodicalIF":0.0000,"publicationDate":"2009-08-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"1","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta pathologica et microbiologica Scandinavica. Section B: Microbiology and immunology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1111/J.1699-0463.1970.TB04312.X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 1
Abstract
Meningococcal extracts mediate an incorporation of 32P in the presence of Mg44 and ADP which is improved by the addition of EDTA. A major part of this incorporation is due to a polynucleotide phosphorylase activity, and is independent of electron flux. But the endogenous respiration is also accompanied by a phosphorylation. When the cytochrome oxidase is inhibited by KCN phosphorylation occurs concomitantly with the endogenous reduction of added mammalian ferricytochrome c. This phosphorylation is nearly doubled when KHCO3 is included in the system. It has not been possible to demonstrate an oxidative phosphorylation on the electron-oxygen transport level in meningococcal extracts with NADH, NADPH or ferrocytochrome c as electron sources. The phosphorylation connected with electron flux, and its enhancement by KHCO3 have been discussed in relation to the CO2 requirements typical for N. meningitidis.