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J Bacteriol. 1968 August; 96(2): 298-305
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Cytochrome c in Hydrogenomonas eutropha¹

^a Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706

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.

² Present address: Research Division, Raychem Corp., Menlo Park, Calif. 94025.

¹ Published with the approval of the Director of the Wisconsin Agricultural Experiment Station.