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Studies with Triton X-100 treated electron transport particles from Rhodospirillum rubrum

Summary

The effects of Triton X-100 on the membranal fraction containing the electron transport system in R. rubrum were studied.

  1. 1.

    The NADH oxidase system is very sensitive to treatment with Triton X-100. An inactivation of 50% is already found with a detergent/membrane protein ratio of 0.012(w/w).

  2. 2.

    NADH-cytochrome c-reductase also becomes very rapidly inactivated.

  3. 3.

    The activity of succinate-cytochrome c-reductase is stimulated by low and inactivated by higher concentrations of Triton X-100. The increase in activity is appr. 200%.

  4. 4.

    NADH dehydrogenase with menadione as electron acceptor is partly inactivated by low concentrations of Triton. Higher concentrations of the detergent will again lead to a stimulation of the activity. In the presence of these higher detergent concentrations the kinetics of the reaction of the enzyme are altered, i.e. an increase of up to 300% of the reaction rate is found during assay. The low initial rate is slowly increased with the time the samples containing Triton are kept at 0° C. Elevated temperatures (20° C) or dilution of the sample prior to assay will cause the initial rate to rise immediately.

  5. 5.

    Succinate dehydrogenase, NADH dehydrogenase with DCPIP, ferricyanide and also the activity with menadione are very stable against treatment with Triton. A detergent/membrane protein ratio of 12.5 will result in only slight inactivation of these activities.

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References

  1. Boll, M.: Oxydation von reduziertem Nicotinamid-Adenin-Dinucleotid in Rhodospirillum rubrum. I. Charakterisierung einer löslichen NADH-Dehydrogenase. Arch. Mikrobiol. 62, 94–110 (1968a).

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  3. —: The effect of deoxycholate on enzymes with electron transport function from Rhodospirillum rubrum. Arch. Mikrobiol. 68, 191–200 (1969a).

  4. —: Oxidation of reduced nicotinamide-adenine-dinucleotide in Rhodospirillum rubrum. III. Properties of a NADH dehydrogenase solubilized from electron transport particles. Arch. Mikrobiol. 69, 301–313 (1969b).

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  6. Lowry, O. H., Rosebrough, M. J., Farr, A. L., Randall, R. J.: Protein measurements with the Folin phenol reagent. J. biol. Chem. 193, 265–275 (1951).

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Boll, M. Studies with Triton X-100 treated electron transport particles from Rhodospirillum rubrum . Archiv. Mikrobiol. 71, 1–8 (1970). https://doi.org/10.1007/BF00412229

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Keywords

  • NADH
  • Ferricyanide
  • Succinate Dehydrogenase
  • Menadione
  • NADH Dehydrogenase