Cytochrome coxidase hasbeenpurified fromZeamaysmitochondria byasolubilization withdodecyl maltoside followed by asimple andrapid twostepfastprotein liquid chromatographic methodinvolving anionexchange onMonoQ andsizeexclusion chromatography onSuperose 12.Thepreparation obtained was resolved byureasodium dodecyl sulfate-polyacrylamide gelelectrophoresis andhadasubunit composition comprising polypeptides ofapparent molecular massesof48,31,and25kilodaltons atleast oneat16and11kilodaltons andthree subunits below10 kilodaltons. Comparison withapurified yeastcytochrome coxidaserevealed thatthefourlargest subunits showedsimilar electrophoretic mobilities. Subunits Iand11cross-reacted with antibodies raised against theyeasthomologous polypeptides. Polypeptides oftheplant ubiquinone:cytochrome c reductase complex havealsobeenidentified bycross-reaction withantibodies raised against yeastcytochrome bandc1subunits and byinference fromcomigration.
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