By H. Baltscheffsky (auth.), Prof. Dr. Günter Schäfer, Prof. Dr. Martin Klingenberg (eds.)
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U f u Vl QJ 15 >. ".... L 100 Cl. u QJ u Vi QJ 01 o 4- o >. ~~~20~~::~4~0~~~J63 Number of gel slice Fig. 5. Dodecyl sulfate gel electrophoresis of the dimeric cytochrome b from cells having incorporated [ 14 cJleucine in the absence of inhibitors and [3 Hl leucine in the presence of cycloheximide or chloramphenicol identification of the cytochrome b subunits among the protein bands obtained by dodecyl sulfate gel electrophoresis of the whole complex was also not possible (Weiss and Ziganke, 1977).
Biophys. : J. Bioenerg. Biomembr. : Arch. Biochern. Biophys. : Biochim. Biophys. : Biochim. Biophys. : Arch. Biochero. Biophys. : Arch. Biochem. Biophys. : FEBS Lett. : Proc. Natl. Acad. Sci. A. : In: Dynamics of Energy Transducing Membranes. C. , 1974, pp. : Proc. Natl. Acad. Sci. A. WEISS Introduction The main energy-transducing enzymes of the mitochondrial inner membrane are organized as distinct multiprotein complexes (Fig. 1), oxidoreductases (complexes I, III, and IV), which transduce the energy generated by multiple oxidation-reduction reactions into an intermediate energy form that can be used by the ATP-synthetase (complex V) for the formation of ATP (for review see Hatefi, 1978).
1976b). , 1976b; Kotylak and Slonimski, 1977; Colson and Slonimski, 1977). The following criteria have been used to establish that two phenotypically similar mutations are closely linked and located in the same locus: 1. When strains with mit- and/or AntR mutations in the same locus are mated, diploid respiratory-competent (mit+) and/or inhibitor-sensitive (Ants) strains are produced at a low frequency (below 1%). The 35 frequency, however, is high (up to 15%) in crosses of mutants belonging to different loci.
Energy Conservation in Biological Membranes by H. Baltscheffsky (auth.), Prof. Dr. Günter Schäfer, Prof. Dr. Martin Klingenberg (eds.)