Autor: |
Hillar, M., Lott, V., Lennox, B. |
Zdroj: |
Journal of Bioenergetics and Biomembranes; March 1975, Vol. 7 Issue: 1 p1-15, 15p |
Abstrakt: |
1.Succinate dehydrogenase is inhibited by citrate and ß-hydroxybutyrate in a complex manner, both in mitochondria and submitochondrial particles. Kinetics of inhibition in the particles points to a competitive component in the mechanism involved.2.Pyruvate, a-ketoglutarate, malate, and glutamate stimulate oxidation of succinate by mitochondria.3.Stimulation by a-ketoglutarate and glutamate is not influenced by the presence of rotenone.4.Stimulation by pyruvate is higher in the absence of rotenone and increases significantly in the presence of K+ and valinomycin. Pyruvate supplies in mitochondria reducing equivalents for malate dehydrogenase operating in the reverse direction-reduction of oxaloacetate to malate.5.Stimulation by malate is higher in the presence of rotenone. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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