Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phenylmercuric acetate can be detected by horse liver acetone powder succinate dehydrogenase inhibition, using a mixture of 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyl tetrazolium chloride (INT), sodium succinate, and N-methylphenazonium methosulfate as the chromogenic reagent. The simple cleanup involves extraction of phenylmercuric acetate in chloroform and concentration by evaporation. In the extract, the compounds in seeds or water could be separated and identified by paper chromatography in the field or laboratory at microgram levels with an acetone-water (70 + 30) solvent system.
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PMID:Simple and rapid portable chromatographic method for separation and detection of phenylmercuric acetate in seeds and water. 646 10

Through a methodological evaluation, reliable histochemical and biochemical methods for succinate dehydrogenase activity in cultured human skin fibroblasts and amniotic fluid cells were developed. The histochemical method includes a cleaning of the cultured cells in 1 mM malonate in 0.9% NaCl, air-drying and fixation in acetone (5 min at -20 degrees C), coating of cells with CoQ10 (0.2 mg/ml in ether/acetone) and incubation for 1 h at 37 degrees C in 50 mM succinate and 0.5 mg/ml Nitro BT in 200 mM phosphate buffer, pH 7.6 PMS as an intermediate electron carrier was found inferior to exogenous CoQ10. Both types of cells exhibit equal activity. In the biochemical method homogenizing was performed in 50 mM Tris-HCl buffer, pH 7.5, and 200 mM sucrose. The standard incubation was 2.0 mM INT and 10 mM succinate in 10 mM Tris-HCl buffer, pH 7.5 for 1 h at 37 degrees C. The apparent Km values for INT and succinate were estimated to 0.39 mM and 0.13 mM, respectively, while I0.5 for malonate was 0.46 mM. Activity in amniotic fluid cells was 18.1 pkat/mg protein and in human skin fibroblasts 20.3 pkat/mg protein. Specificity of the methods was tested by use of a Chinese hamster fibroblast strain B9 known to be succinate dehydrogenase deficient in addition to various control experiments. Congruent results were obtained with the two methods.
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PMID:Succinate dehydrogenase activity in cultured human skin fibroblasts and amniotic fluid cells. A methodological study. 687 23

An improved spectrophotometric method for measuring succinate dehydrogenase (EC 1.3.99.1) activity with the use of 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride (INT) is described. The procedure has been evaluated in mitochondrial fractions and homogenates of frog skeletal muscle. For mitochondrial suspensions, extraction of formazan with alcohol was found to be superior to extraction with ethyl acetate. For homogenates, complete extraction of formazan required sequential treatment with alcohol and ethyl acetate; the generally employed procedure of extracting once with ethyl acetate alone led to serious underestimation of the amount of formazan in the tissue. Observations of mitochondrial suspension incubated with various concentrations of INT led to the selection of 0.8 mM INT for optimal results. Higher concentrations, although commonly used, can exert undesirable inhibitory effects on succinate dehydrogenase activity, especially at low concentrations of mitochondria and after longer periods of incubation. The problem of instability of succinate dehydrogenase was solved by the addition of buffer at pH 7.5.
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PMID:Assay of succinate dehydrogenase activity by the tetrazolium method: evaluation of an improved technique in skeletal muscle fractions. 696 45

Changes in the histochemical profile of 43 rat extensor digitorum longus muscles undergoing de-innervation and re-innervation were recorded. Assessment of fibre type composition and muscle fibre cross-sectional area was performed at 15, 30, 90 and 180 days post operative (p.o.) after either primary end-to-end repair or autologous graft repair of the common peroneal nerve (n = 5 per time point and type of repair). The size and histochemical profile of single muscle fibres were analysed by computer-assisted quantification on the basis of their myofibrillar ATPase (pH 4.3) and succinate dehydrogenase (SDH) activities in serial, whole-muscle cross-sections. Accordingly, four muscle-fibre types could be functionally identified: (1) slow oxidative (SO, type I); (2) fast-oxidative glycolytic (FOG, type IIA); (3) fast glycolytic (FG, type IIB); and (4) succinate dehydrogenase intermediate (SDH-INT). At 15 days following end-to-end repair, the SDH-INT muscle fibre type was observed. By contrast, 15 days following graft repair, no changes in fibre type composition were observed (vs. control). At 30 days p.o. in the group that received end-to-end repair, type SDH-INT reached its maximum and was significantly higher than in the group that underwent graft repair. At 90 days p.o., the amount of SDH-INT fibres declined after end-to-end repair, but it was still significantly higher than in the group treated with a nerve graft. The increase of the SDH-INT fibre type was mirrored by a proportional disappearance of FG and FOG fibres. These changes were time-dependent, not reversible at 180 days p.o and largely blunted after nerve graft. Muscle-fibre size decreased at 15 and 30 days after both types of nerve repair. This decrease was transient and reversible within 90 days p.o. These findings reflect the fact that the reorganization of the histochemical profile in re-innervated muscles is both time dependent and long lasting. The degree of this reorganization is significantly higher after end-to-end repair than after graft repair.
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PMID:Histochemical alterations of re-innervated rat extensor digitorum longus muscle after end-to-end or graft repair: a comparative histomorphological study. 1289 4