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

In the present investigations, the localization of several enzymes (Acid Phosphatase, Peroxidase, succinic dehydrogenase, Phosphorylase, alkaline phosphatase, ATP-ase) and other substances in the guard and subsidiary cells as well as trichomes of the leaves of Phaseolus mungo, was carried out. Attempts were also made to follow the sequence of developmental stages starting with meristemoids and culminating in differentiated structures. The basic information thus obtained is used in interpreting the developmental physiology of stomatal differentiation as well as their cellular organisation. Histochemical observations made in the present studies are compared with the electron microscopical observations of Whatley (1972). It is proposed that mitochondria played a basic role in the functioning of the guard cells. The present studies also demonstrated activity of acid phosphatase in the guard cells and was localized in spherosomes. The latter varied in the activity for acid phosphatase and was dependent on the turgid level of the cell. Interestingly, enough localization of phosphatase could only be observed in spherosomes when the osmotic pressure in the cell was relatively low, once the osmotic pressure increased, the activity disappeared.
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PMID:Histochemical studies in stomatal apparatus of Phaseolus mungo Linn. I. Localization of enzymes and structural material. 12

The histoenzymatic characteristics of regenerating myofibers of rat masseter muscle following injection of 1% lidocaine, as well as morphometric and histochemical characteristics of the typical myofibers, were investigated. Myoblasts appeared initially by day 1 among numerous macrophages within the confines of degenerating myofibers. Myotubes predominated by the 3rd day. Complete regeneration of the muscle occurred by at least 45 days. Phosphorylase activity was absent at day 1 and reappeared by the 5th day when the regenerating myofibers showed slight activity. By the 15th day the myofiber types had partly differentiated; red myofibers were smaller and stained less intensely than the white myofibers. Myotubes stained uniformly for succinic dehydrogenase activity from 3 until 5 days. After 5 days this staining increased gradually. Myofiber types began differentiation by 15 days and were fully differentiated by 45 days. ATPase activity was barely evident by 1-3 days. This activity appeared uniformly low up to 5 days and increased to an intensity comparable with that of the typical myofiber by 15 days. Slight leucine aminopeptidase activity occurred in macrophages 1 day following injection. By 3 days this activity appeared in the remaining myoblasts and in the myotubes. Some activity was found in the fibroblasts. This staining intensity at 5 days was equal to that of earlier lesions. A trace of this activity was found at 7 days, and none at 15 days. Glucose-6-phosphate dehydrogenase activity was present in the macrophages by day 1. It increased by 3 days and occurred mainly in myoblasts and myotubes. This activity decreased by 5 days, and none was found by 7 days.
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PMID:Regeneration of masseter muscle following lidocaine-induced degeneration. A histochemical study. 14 12

The authors have studied the enzymhistochemical and ultrastructural pictures of tenocytes of adult human tendons. High succinate dehydrogenase, cytochrome oxidase, TPN-diaphorase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity were found, as indicated both oxidativ, anaerobic and pentose-phosphate shung activity. Phosphorylase and glutamate dehydrogenase activity was medial, lipase and alcaline phosphatase activity was slight. In tenocytes well developed rough endoplasmic reticulum and GOLGI apparatus, large amount of free ribosomes were found.
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PMID:Histochemical and ultrastructural study of adult human tendon. 23 84

The effects of cadmium chloride (Cd) alone (1 mg given as a single injection) or in combination with ascorbic acid (AA; 100 mg/day for 10 days) on the secretory functions of sex accessory glands of rats were studied in healthy male albino rats. Animals were sacrificed after 10 days treatment and the seminal vesicles (SVs), dorsolateral prostate (DLP), ventral prostate (VP), bulbourethral glands (BU), and coagulating glands (CO) were excised and weighed. Weight of all accessory glands were decreased by 10 days treatment with Cd. Cd + AA gave similar results. AA concentration increased in all glands and was significantly increases in CO (p less than .01). Levels of ascorbogin increased in all glands except CO and BU and in the latter a significant (p less than .001) increase was found. The rate of AA utilization increased significantly (p less that .001) in the accessories. A significant (p less than .001) reduction in the activity of succinate dehydrogenase was observed in Cd-treated rats with a further reduction with combined treatment. Alkaline phosphatase decreased (p less than .001) after Cd treatment but AA in combination restored it to control levels. Cd increased acid phosphatase (p less than .001) and was further activated by Cd + AA. Phosphorylase activity was elevated with Cd (p less than .001) but recovery occurred in SV and BU with Cd + AA. Glycogen increased (p less than .001; .01) with both treatments as did citric acid. Protein results were inconsistent with Cd but activation was found in most glands under combined treatment. The results reveal that most androgen-dependent biochemical constituents and organ weights were affected significantly by a single injection of Cd. AA had a protective and beneficial influence on the restoration of structural integrity and metabolism in sex accessory glands.
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PMID:Effects of CdCl2 on the secretory functions of sex accessory glands of rats. 60 64

All birds have a glial enclosed, glycogen-containing structure in the lumbosacral region of their spinal cords. Recently, a dorsal, central, glycogen-rich area surrounding the central canal in the brachial spinal cord was described in domestic chickens. In order to topographically delineate and histochemically describe this structure, fresh, frozen serial sections of chicken brains and spinal cords were processed for glycogen content, phosphorylase, succinic dehydrogenase and cholinesterase activities. The glycogen-rich area surrounding the central canal in the lumbosacral region is found at all levels of the spinal cord and lower medulla. In the upper medulla, it is located in the medline floor immediately ventral to the ependyma. It persists in this position until the level of the oculomotor complex where it ends. Phosphorylase positive regions closely parallel the glycogen distribution. No succinic dehydrogenase or cholinesterase activities are found in these areas.
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PMID:The craniocaudal extent of the glycogen body in the domestic chicken. 89 22

1. Cross sections from the middle of the gluteus medius were removed from 10 adult horses and used to evaluate changes in histochemically determined muscle fiber type and biochemically determined metabolic enzyme activities as a function of sample depth. 2. Muscle fiber types determined using histochemical methods for myosin ATPase (pH 9.4) and succinic dehydrogenase (SDH) activity indicated percent fast-twitch glycolytic (FG) muscle fibers decreased and slow-twitch oxidative (SO) fibers increased as a function of increasing sampling depth. 3. Percent histochemically determined fast-twitch oxidative glycolytic (FOG) fibers decreased slightly only in the deepest region of the gluteus medius. 4. Citrate synthase (CS) enzymatic activity, used as a marker for mitochondrial oxidative potential, increased 2.5-fold in activity per g of muscle protein from 1 to 8 cm sampling depth. 5. 3-hydroxyacyl-CoA dehydrogenase (HAD) enzymatic activity, used as a marker for lipid oxidation potential, increased 3-fold in activity per g of muscle protein when the depth increased from 1 to 8 cm. 6. Phosphorylase (PS) enzymatic activity, used as a marker for potential glycogen utilization, decreased 50% in activity per g of muscle protein when going from 1 to 8 cm. 7. Lactate dehydrogenase (LDH) enzymatic activity, used as a marker for anaerobic glycolytic potential, decreased about 50% in activity as the sampling depth increased from 1 to 8 cm. 8. In summary, the superficial portion of the equine gluteus medius was found to be more glycolytic and less aerobic in its metabolic profile than deeper regions. The muscle became progressively more aerobic and less glycolytic with increasing sampling depth.
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PMID:Changes in the metabolic profile of the equine gluteus medius as a function of sampling depth. 290 49

Muscle biopsies were obtained from three cyclists and four runners at the end of 10-24 mo of intensive training and after intervals of detraining up to 12 wk. Control samples came from four untrained persons and four former athletes. Macro mixed fiber samples were assayed for lactate dehydrogenase, adenylate kinase, glycogen phosphorylase, citrate synthase, malate dehydrogenase, beta-hydroxyacyl-CoA dehydrogenase, succinate dehydrogenase, beta-hydroxybutyrate dehydrogenase, creatine kinase, hexokinase, 1-phosphofructokinase, fructosebisphosphatase, protein, and total creatine. In the case of three trained persons and two controls, the first six of the enzymes were also measured in individual fibers. Before detraining, enzymes of oxidative metabolism were substantially higher than in controls, and differences in levels between type I and type II fibers were smaller. During detraining, oxidative enzymes were decreased in both fiber types but the type II fibers did not fall to control levels even after 12 wk. Phosphorylase increased with detraining in both fiber types. The same is true for lactate dehydrogenase and adenylate kinase, except in the case of the type I fibers of one individual. Among the other six enzymes (measured in mixed fiber samples), only hexokinase was consistently affected (decreased) by detraining.
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PMID:Effects of detraining on enzymes of energy metabolism in individual human muscle fibers. 682 50