The effect of temperature and anoxia of kidney on the subsequent oxidative phosphorylation of mitochondria
- 1 January 1967
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 102 (1) , 48-52
- https://doi.org/10.1042/bj1020048
Abstract
[Rat] kidneys were kept anoxic at 4[degree], 20[degree] and 38[degree]. Mitochondria were then isolated and their oxidative phosphorylation and respiration were determined. Under all conditions the rate of phosphate esterification was affected to a greater extent, or earlier, than oxygen consumption. Glutamate and succinate were used as substrates. The depression of p/O ratio was greater for glutamate at 4[degree], and for succinate at 20[degree]. Anoxia abolished the inhibiting effect of fluoride on respiration. Fhosphate esterification, after anoxia, was higher in the presence of fluoride than its absence, whereas in control preparations they were the same. The decrease in P/O ratio did not appear to be due to activation of adenosine triphosphatase, as activities of both Mg2+- and dinitrophenol-activated adenosine triphosphatases were decreased after anoxia.This publication has 6 references indexed in Scilit:
- The effect of temperature and anoxia of rat-kidney slices on their subsequent respirationBiochemical Journal, 1967
- Stability of Oxidative Phosphorylation and Related Reactions in Isolated Liver MitochondriaJournal of Biological Chemistry, 1959
- OXIDATIVE PHOSPHORYLATION BY AN ENZYME COMPLEX FROM EXTRACTS OF MITOCHONDRIA .4. ADENOSINETRIPHOSPHATASE ACTIVITY1957
- LATENT ADENOSINETRIPHOSPHATASE ACTIVITY IN RESTING RAT LIVER MITOCHONDRIAJournal of Biological Chemistry, 1953
- Determination of Inorganic PhosphateAnalytical Chemistry, 1949
- INTRACELLULAR DISTRIBUTION OF ENZYMES .3. THE OXIDATION OF OCTANOIC ACID BY RAT LIVER FRACTIONS1948