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Origin of mitochondrial enzymes. V. The polypeptide character and the biosynthesis of rat liver cytochromec oxidase polypeptides by mitochondria

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Abstract

Isolated rat liver mitochondria were labeled in vitro withl-[14C]leucine. Sixty percent of the incorporated radioactivity was found to reside in subunits 1, 2, and 3 of cytochromec oxidase with apparent molecular weights of approximately 33,000, 25,000, and 20,000, respectively. The results indicate that these are the predominant products of protein synthesis under the conditions employed. The enzyme complex, as derived by immunoprecipitation, was found to contain four additional polypeptides with apparent molecular weights of 17,000, 12,500, 7000, and 3500. A comparison of electrophoretic profiles of the rat liver and beef heart enzyme reveals that the apparent molecular weights of all polypeptides are remarkably similar.

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Authors and Affiliations

  1. Department of Biochemistry and Nutrition School of Medicine, University of North Carolina, 27514, Chapel Hill, North Carolina

    Jerome D. Bernstein, John R. Bucher & Ralph Penniall

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  1. Jerome D. Bernstein
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  2. John R. Bucher
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  3. Ralph Penniall
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To be submitted as partial fulfillment of the requirements for the Ph.D. degree of this institution.

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Bernstein, J.D., Bucher, J.R. & Penniall, R. Origin of mitochondrial enzymes. V. The polypeptide character and the biosynthesis of rat liver cytochromec oxidase polypeptides by mitochondria. J Bioenerg Biomembr 10, 59–74 (1978). https://doi.org/10.1007/BF00743227

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  • DOI: https://doi.org/10.1007/BF00743227

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