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1、Biochem.J.(2003)375,3340(PrintedinGreatBritain)33Characterizationofnon-covalentoligomersofproteinstreatedwithhypochlorousacidAnnaL.P.CHAPMAN*,ChristineC.WINTERBOURN*1,StephenO.BRENNAN†,T.WilliamJORDAN‡andAnthonyJ.KETTLE**FreeRadicalResearchGroup,DepartmentofPathology,ChristchurchSchoolo
2、fMedicineandHealthSciences,P.O.Box4345,Christchurch,NewZealand,†MolecularPathologyLaboratory,ChristchurchHospital,Christchurch,NewZealand,and‡SchoolofBiologicalSciences,VictoriaUniversity,Wellington,NewZealandHypochlorousacid(HOCl)isapotentoxidantproducedbyConversionofpositivelyintonega
3、tivelychargedgroupsonmyeloperoxidasethatcausesaggregationofmanyproteins.Treat-theproteinbysuccinylationcausedpreformedaggregatestomentofapohaemoglobinandapomyoglobinwithHOClproduceddissociate.Treatmentofapomyoglobinwithtaurinechloraminearegularseriesofoligomerbandswhentheproteinsweregen
4、eratedmethioninesulphoxidesbutfewproteincarbonyls,separatedbySDS/PAGEunderreducingconditions.Aggregationanddidnotresultinaggregation.WeconcludethataggregationwasdetectableataHOCl/proteinmolarratioof0.5:1andwaswasduetostrong,non-covalentinteractionsbetweenproteinmaximalatratiosof10:120:1
5、.Dimersformedwithin1minofchains.WeproposethatformationofproteincarbonylsandaddingHOCl,andfurtheraggregationoccurredoverthenextpossiblychloramines,alongwithmethionineoxidation,alters30min.Noconvincingevidenceforcovalentcross-linkingwasproteinfoldingtoexposehydrophobicareasonneighbouringo
6、btainedbyaminoacidanalysis,peptideanalysisorelectrospraymoleculesthatassociatetoformdimersandhigher-molecular-ionization-MSofHOCl-modifiedapomyoglobin.Thelattermassaggregates.Thisprocesscouldleadtotheformationofshowedanincreaseinmassconsistentwithconversionofthetwoaggregatedproteinsatsit
7、esofmyeloperoxidaseactivityandmethionineresiduesintosulphoxides.A5-foldexcessofHOClcontributetoinflammatorytissueinjury.generatedapproximatelythreechloraminesontheapomyoglobin.Theseunderwentslowdecay.ProteincarbonylswereformedKeywords:haemoglobin,myeloperoxidase,myoglobin,neutro
