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. 1968 Aug;96(2):298–305. doi: 10.1128/jb.96.2.298-305.1968

Cytochrome c in Hydrogenomonas eutropha1

Florence S Fang a,2, R H Burris a
PMCID: PMC252297  PMID: 4970645

Abstract

A c-type cytochrome from Hydrogenomonas eutropha was purified 150-fold by butanol extraction, ammonium sulfate precipitation, and column chromatography. Three distinct c-type cytochromes were recovered which did not bind with either carbon monoxide or cyanide and hence did not appear to be denatured. Polyacrylamide gel electrophoresis indicated that one protein was acidic and the other two were basic. The acidic cytochrome c had a sedimentation coefficient of 3.46. Its amino acid composition was not markedly different from other bacterial cytochromes, but relative to mammalian cytochromes c it was low in lysine, threonine, and isoleucine and high in alanine and valine.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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