Literature DB >> 210176

The use of orthacryl two-dimensional polyacrylamide gel electrophoresis to identify and compare the subunit polypeptides of bovine heart and yeast cytochrome c oxidases.

R O Poyton, E McKemmie, C George-Nascimento.   

Abstract

A two-dimensional electrophoretic method which takes advantage of the "migration anomalies" experienced by some polypeptides on gels of different porosities has been successfully used to resolve the seven subunit polypeptides of yeast cytochrome c oxidase and the nine polypeptides associated with bovine cytochrome c oxidase. The two-dimensional maps provided by this method reveal clear differences between these two cytochrome c oxidases.

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Year:  1978        PMID: 210176

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

Review 1.  Interactions in cytochrome oxidase: functions and structure.

Authors:  J A Freedman; S H Chan
Journal:  J Bioenerg Biomembr       Date:  1984-04       Impact factor: 2.945

2.  Additional components of bovine heart cytochrome c oxidase demonstrated by high-resolution polyacrylamide-gel electrophoresis in the presence of chloral hydrate.

Authors:  D C Griffin; M Landon
Journal:  Biochem J       Date:  1981-08-01       Impact factor: 3.857

  2 in total

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