Abstract
Using succinate and α-ketoglutarate as substrates, oxidative phosphorylation has been measured in mitochondria isolated from livers showing cloudy swelling. This cellular change was obtained by injecting rats with S. typhi murium toxin and guinea pigs with diphtheria toxin. It has been found that phosphorylation associated with the oxidation of either of these substrates was partially inhibited in mitochondria from livers showing cloudy swelling, while the oxygen consumption was unchanged. Thus, the P:O ratios for both succinate and α-ketoglutarate were lower in mitochondria from treated animals than they were in normal mitochondria. Dephosphorylation of ATP was not significantly modified in mitochondria from livers showing cloudy swelling as compared with normal controls. No dephosphorylation of AMP and G-6-P was observed either in normal mitochondria or in mitochondria from treated animals.
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- Bailey K., Webb E. C. Purification of yeast hexokinase and its reaction with betabeta'-dichlorodiethyl sulphide. Biochem J. 1948;42(1):60–68. doi: 10.1042/bj0420060. [DOI] [PMC free article] [PubMed] [Google Scholar]
- COPENHAVER J. H., Jr, LARDY H. A. Oxidative phosphorylations; pathways and yield in mitochondrial preparations. J Biol Chem. 1952 Mar;195(1):225–238. [PubMed] [Google Scholar]
- DIANZANI M. U. Uncoupling of oxidative phosphorylation in mitochondria from fatty livers. Biochim Biophys Acta. 1954 Aug;14(4):514–532. doi: 10.1016/0006-3002(54)90232-2. [DOI] [PubMed] [Google Scholar]
- FONNESU A., SEVERI C. La fosforilazione del glicoso nel coniglio difterico. Boll Soc Ital Biol Sper. 1952 Dec;28(12):1923–1925. [PubMed] [Google Scholar]
- FONNESU A., SEVERI C. Lesioni cellulari nell'intossicazione cronica da 2,4-dinitrofenolo. Arch Sci Biol (Bologna) 1954 Nov-Dec;38(6):597–606. [PubMed] [Google Scholar]
- HARMAN J. W., KITIYAKARA A. Studies on mitochondria. VI. The relationship between the structure, osmotic reactivity and ATPase activity of mitochondria from pigeon skeletal muscle. Exp Cell Res. 1955 Jun;8(3):411–435. doi: 10.1016/0014-4827(55)90119-1. [DOI] [PubMed] [Google Scholar]
- KALTENBACH J. C., HARMAN J. W. Studies on mitochondria. VII. The relationship between the control of structure and the dinitrophenol stimulation of adenosinetriphosphatase in liver mitochondria. Exp Cell Res. 1955 Jun;8(3):435–452. doi: 10.1016/0014-4827(55)90120-8. [DOI] [PubMed] [Google Scholar]
- KIELLEY W. W., KIELLEY R. K. Myokinase and adenosinetriphosphatase in oxidative phosphorylation. J Biol Chem. 1951 Aug;191(2):485–500. [PubMed] [Google Scholar]
- Keilin D., Hartree E. F. Purification and properties of cytochrome c. Biochem J. 1945;39(4):289–292. doi: 10.1042/bj0390289. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LARDY H. A., WELLMAN H. The catalytic effect of 2,4-dinitrophenol on adenosinetriphosphate hydrolysis by cell particles and soluble enzymes. J Biol Chem. 1953 Mar;201(1):357–370. [PubMed] [Google Scholar]
- POTTER V. R., SIEKEVITZ P., SIMONSON H. C. Latent adenosinetriphosphatase activity in resting rat liver mitochondria. J Biol Chem. 1953 Dec;205(2):893–908. [PubMed] [Google Scholar]
- WITTER R. F., NEWCOMB E. H., STOTZ E. Studies of the mechanism of action of dinitrophenol. J Biol Chem. 1953 May;202(1):291–303. [PubMed] [Google Scholar]