Studies on Cytochrome <i>b</i>:III. Comparison of Cytochrome <i>b</i>'s from Beef Heart Muscle and Larvae of the Housefly

  • OHNISHI KEN
    Department of Biology, Faculty of Science, University of Osaka

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1. The GO-affinity of the cytochrome b's from housefly larvae and beef heart muscle were discussed.<br> 2. Preliminary analyses of the amino acid compositions of the two cytochrome b's were made. The molecular weight obtained by these analyses were in good agreement with those obtained by other methods. The contents of hydrophobic residues in the two cytochromes were compared.<br> 3. By ultracentrifugal studies, it was found that the beef heart cytochrome b pre-paration was made up of aggregates, whereas the purified preparation of larval cytochrome b was monomeric.<br> 4. Beef heart cytochrome b could be reduced with NADH in the presence of yeast NADH-cytochrome c reductase but larval cyto-chrome b had no affinity for this enzyme system.<br> 5. The. oxidation-reduction potentials of the two cytochromes were determined. The E0' value of beef heart cytochrome b was lower than that of larval cytochrome b.<br> The author wishes to thank Prof. K. Okunuki for his valuable advice during this work and Dr. H. Matsubara and Dr. Y. Orii for their technical guidance in amino acid and ultracentrifugal analyses.

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