Succinic dehydrogenase activity

Figure 11. (a) Succinate dehydrogenase activity in normal skeletal muscle, (b) Muscle from patient with complex 11 deficiency showing severely decreased succinate dehydrogenase activity. 

In addition to binding to cytochrome c oxidase, cyanide inhibits catalase, peroxidase, methemoglobin, hydroxocobalamin, phosphatase, tyrosinase, ascorbic acid oxidase, xanthine oxidase, and succinic dehydrogenase activities. These reactions may make contributions to the signs of cyanide toxicity (Ardelt et al. 1989 Rieders 1971). Signs of cyanide intoxication include an initial hyperpnea followed by dyspnea and then convulsions (Rieders 1971 Way 1984). These effects are due to initial stimulation of carotid and aortic bodies and effects on the central nervous system. Death is caused by respiratory collapse resulting from central nervous system toxicity. 

Because the metabolism of DEHP was catalyzed by so many fractions of the trout liver homogenate, these fractions were characterized by measurement of marker enzymes to determine which organelles actually were responsible for the observed DEHP metabolism. Succinic dehydrogenase activity was used as a marker for mitochondria, whereas glucose-6-phosphatase was used as a marker for microsomes. The distribution of DEHP oxidase activity (production of polar metabolites 1 and 2 with added NADPH) and of DEHP esterase activity (production of monoester without added NADPH) were also determined. It was found (Figure 2) that the distribution of DEHP oxidase activity parallels the distribution of microsomal activity and the distribution of DEHP esterase activity parallels the distribution of microsomal activity, but is also present in the cytosol fraction. 

Gasper GM and Kawatski JA. 1972. Inhibition by heptachlor epoxide of succinic dehydrogenase activity in mouse liver homogenates. Comp Biochem Physiol 41 655-660. 

Hazel, J.R. (1972). The effect of temperature acclimation upon succinic dehydrogenase activity from the muscle of common goldfish lipid reactivation of the soluble enzyme. Comparative Biochemistry and Physiology 43B, 863-882. 

Shchepkin, V.Ya. (1978). The study of succinate dehydrogenase activity of white skeletal, red muscles and liver in fish with different ecological and physiological peculiarities (In Russian). Biologiya Morya, Kiev 46,104-107. 

Organelle Preparation Succinate Dehydrogenase Activity (% of total)... 

Succinic Dehydrogenase Activity, Determination of (Singer and Kearney). 4... 

Hearn, G. R. and Walnlo, W. W. (1956) Succinic dehydrogenase activity of the heart and skeletal muscle of exercise rats. 

Fra. 33. Activation of succinate dehydrogenase by NADH. A preparation of phos-phorylating submitochondrial particles (ETPh) (succinoxidase activity = 1.18 /unoles succinate per min per mg at 30°) was washed by centrifugation in a sucrose-Tris-Mg buffer (pH 7.4) and resuspended in the same buffer at 1 mg of protein/ml. Antimycin A (1 nmole/mg protein) was added to slow the rate of aerobic oxidation of NADH, followed by 0.25 mAf NADH. Oxidation of the latter at 23° was monitored spectro-photometrically at 340 nm (dashed line). Samples were removed periodically and assayed immediately for succinate dehydrogenase activity in the presence of 033 mg of PMS/ml (solid line). At 16 min a second aliquot of 035 mM NADH was added. From Gutman et al. (197). 

Succinate Dehydrogenase. Activity is determined by a modification of the procedure of Hiatt. The reaction mixture contains, in a final volume of... 

The succinate dehydrogenase of S. acidocaldarius (DSM 639) is located in the cytoplasmic and membrane fractions when cells are disrupted either by sonication or decompressive disruption. About 10-30% of the activity is associated with the membrane fraction [30]. The purified membrane-bound succinate dehydrogenase activity (M, 141 000) consists of four subunits (Mr 66000, 31 000, 28 000, and 12,800). The enzyme contains a covalently-bound flavin as well as iron and acid-labile sulfide but no cytochrome [111]. The dehydrogenase reduces the following acceptors (listed in order of decreasing... 

Kato and coworkers have made an extensive study of the mechanism of action of cord factor (see p. 210) and have found a significant decrease of the activity of the succinic and malic dehydrogenase systems of the liver of mice, about twenty-four hours after intraperitoneal injection of 0.1 mg. This finding seems to be related to the work of Martin and coworkers, who reported a decrease of succinic dehydrogenase activity in the kidneys of tuberculous guinea-pigs. 

M2). Pennington (P5) found a similar activity of succinate-tetrazoliura reductase in mitochondria from normal and dystrophic mouse muscle. Succinate dehydrogenase activity has been recently reported to be normal in muscle from patients with dystrophia myotonia (B7). Muscle mitochondria from hamsters in the late stages of hereditary muscular dystrophy have a low rate of oxygen uptake with pyruvate and fumarate as substrates, but not with succinate (J2). 

B7. Bjomtorp, P., Grimby, G., Lindholm, B., Stenberg, J., and Orndahl, G., Succinic dehydrogenase activity in skeletal muscle of normals and patients with dystrophia myotonia. Acta Med. Scand. 188, 273-276 (1970). 

Having a lifetime of two weeks, the sensor was capable of determining NADH and succinate with a linear range up to 0.13 and 0.15 mmolA, respectively. Competitive inhibition of the mitochondrial succinate dehydrogenase activity by malonate resulted in a totally selective sensor for NADH.In this way the selectivity enhancement of HIS sensors by inhibition of interfering metabolic routes was demonstrated. 

Aqueous extracts of cat s claw were tested for cytotoxicity in four in vitro bioassays using Chinese hamster ovary cells and bacterial cells (Santa Maria et al., 1997). Concentrations of 10, 20, 30, 40, 50, 75, and 100 mg/mL were used. The neutral protein assay (measures inhibition of cell growth), the total protein content assay, the tetrazolium assay (measures mitochondrial succinic dehydrogenase activity), and the microtox assay (measures inhibition of light output from a luminescent bacterium) showed no evidence of cytotoxicity. 

There were two clearly separated peaks, C and D, sedimenting at 1.2 M and 1.3 M-sucrose (Fig. 2). Examination by the electron microscope showed them both to have the morphological characteristics of synaptosomes. It is well established that a good enzyme marker for intact synaptosomes is occluded lactic dehydrogenase (L-lactate NAD oxidoreductase, EC 1.1.1.27) (Marchbanks, 1967), a component of the cell sap. As can be seen in Table I, 83 % of the occluded form of the enzyme of the original P2 fraction is shared between peaks C and D. Both also contained succinic dehydrogenase activity owing to the presence of intraterminal mitochondria. The membrane marker acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) was also present in these peaks and was notably absent from the mitochondrial and lysosomal fractions (Table I). 

Singer, Thomas P., and Kearney, Edna B., Determination of Succinic Dehydrogenase Activity 4 307... 

Guruprasada Rao, M., Nandakumar, N.V., 1982. The tannery industrial effluent effect on succinate dehydrogenase activity pattern in a freshwater snail Pita globosa. Proc. Ind. Acad. Sci. 91, 427 31. 

Nachlas, M.M., Margulies, S.I., Seligman, A.M., 1960. A colorimetric method for the estimation of succinate dehydrogenase activity. J. Biol. Chem. 235, 499,... 

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