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)

The activities of succinate dehydrogenase (SDR) and lactate dehydrogenase (LDH) as well as the ribonucleic acid levels in the epithelium of both the lactic ducts and alveoli of lactic glands were examined in heifers, close to full term, lactating cows, some of them with subclinical mastitis lesions, and udder biopsies of two cows. The activities of SDH and LDH as well as RNA levels were pronounced in the glandular epithelium of alveoli and in the epithelium of the lesser lactic ducts. All three parameters were also pronounced but at lower levels in the cells of the apical stratum of the two-layer epithelium in the greater lactic ducts. Relationships were found to exist between the enzyme activities and RNA levels and the lactation cycle. Their patterns and manifestations were more or less typical of those areas of the lactic gland which were affected by mastitis.
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PMID:[Histochemical behavior of succinate dehydrogenase and lactate dehydrogenase as well as ribonucleic acid in the epithelium of lactic ducts and alveoli of cow udder]. 9 87

The activities of the Na+--K+-ATPase, succinic dehydrogenase (SDH/, lactic dehydrogenase (LDH/ and glucose-6-phosphat dehydrogenase (G-6-PDH/ were studied in the cortex outer and inner medulla of the kidneys of rats with spontaneous hypertension (SHR) and were compared with those of control normotensive Wistar rats. The SHR aged 6--8 weeks had durint the prehypertensive and the early hypertensive stage the same enzymatic activities as control rats. Rats with a steady SH aged 16-22 weeks had low specific activity of the, Na+--K+-ATPase, SDH and LDH in the outer medulla. The latter can be associated with decreased intensity of the energy metabolism and a reduction of the active sodium transport in the ascending limb of the loop of Henle in the SHR rats and cold cause the phenomenon of exaggerated natriuresis characteristic of hypertension.
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PMID:[Na+--K+-adenosine triphosphatase and some oxidoreductases in the kidney of rats with spontaneous hypertension]. 12 6

Histochemical fibre types classified in sections stained for succinic dehydrogenase (sdh) and myosin ATPase at pH 9.4, were found to be distributed in a consistent manner within the extensor digitorum longus (EDL) and 4 soleus muscles of the adult rat. Simple morphometric techniques applied to complete transverse sections of both muscles showed that the relative distributions and proportions of fibre types along their deep to superficial, and medial to lateral, axes varied accoording to the histochemical method used for fibre typing. Similar differences occurred when the relative ranges of size exhibited by each fibre type were compared in sections stained for SDH and ATPase, and the discrepancies in fibre classification were confirmed by an analysis of individual fibres in serial sections. The findings are discussed in relation to those previosly reported for the EDL and soleus muscles of the rat.
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PMID:The distribution and relative sized of fibre types in the extensor digitorum longus and soleus muscles of the adult rat. 14 Jan 60

Fifty extensor digitorium longus muscles of 25 cats were autografted, 33 with and 17 without prior denervation. After 50 days, no significant differences were observed between predenervated and nonpredenervated autografts. Autografted muscles weighed 48% of the weight of control muscles. Few original muscle fibers survived and within 2 wk autografts contained regenerating muscle fibers. The mean cross-sectional area of muscle fibers in the autografts reached 125% of the value for control nontransplanted muscles. The mean percentage of fibers classified high oxidative in autografted muscles was 67% of values for control muscles. SDH activity of autografted muscle homogenates reached 55% of control values. Up to 60 days after surgery autografts had only fast-twitch fibers. At 170 days autografts remained 95% fast twitch in composition. Revascularization began within 4 days, but the capillary to fiber ratio of long term autografts reached only 60% of control values. Although fiber hypertrophy suggests that cats use autografted muscles, lower than control succinate dehydrogenase activity may result from altered recruitment.
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PMID:Free autografting of entire limb muscles in the cat: histochemistry and biochemistry. 14 61

This study was performed to obtain a more precise quantitative estimation of oxidative and glycolytic potentials and stores of various substrates of the muscles in the human foetus. The material consisted of muscle samples from different muscles, a total of 166 muscle specimens from 65 foetuses and 55 skeletal muscle specimens from 53 infants and children. The latter samples were obtained at surgery. The activities for succinate dehydrogenase and phosphofructokinase were chosen as markers for mitochondrial and cytoplasmatic enzymes respectively. Glycogen, triglyceride and phosphagen levels were studied. Water and protein content of the muscle tissue undergo continuous changes during foetal life and were therefore also included in the study. The SDH activity was low during gestation and reached a value of 2-3 mmoles/kg w.wt. X min at delivery. The PFK activity was also low during gestation, but around 25 weeks gestation a value of 3-4 mmoles/kg w.wt. X min was common, and around delivery time about 7 mmoles/kg w.wt. X min. At 1-5 years the PFK activity was around 11-12 mmoles/kg w.wt. X min, which is similar to adult muscles. Glycogen content varied, but increased during gestation. In the last trimester of gestation a value of 62-92 mmoles units/kg w.wt. was found. The triglyceride content at the end of the gestation time was 3-16 mmoles glycerol/kg w.wt. The phosphagen levels were quite low all through foetal life, averaging between 0.5 and 3 mmoles/kg for ATP and CP concentrations.
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PMID:Some quantitative biochemical evaluations of developing skeletal muscles in the human foetus. 15 52

A method is described which permits the selection of mutants of Neurospora crassa that are deficient in succinic dehydrogenase activity. The method relies on the observation that succinic dehydrogenase-deficient strains fail to reduce the dye nitrotetrazolium blue when overlaid with the dye in the presence of succinate and phenazine methosulfate. Wild-type colonies reduced the dye and turned blue, whereas mutant colonies remained colorless. In this communication we present studies of a mutant, SDH-1, isolated by this method. The mutant had 18% of the succinic dehydrogenase activity of the parent strain used in the mutation experiments as determined from the ratio of Vmax activities obtained from Lineweaver-Burk plots. The SDH-1 mutant segregated in a Mendelian manner when back-crossed to its parent strain. Succinate oxidase activity in SDH-1 was low and was markedly inhibited by adenosine 5'-diphosphate. The succinate oxidase activity of the parent strain was high and was not affected by the presence of adenosine 5'-diphosphate.
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PMID:Selection of succinic dehydrogenase mutants of Neurospora crassa. 15 10

In native cryostat tissue sections of adult female albino rat liver the activities of succinate dehydrogenase (E. C. 1.3.99.1), glucose-6-phosphatase (E. C. 3.1.3.9) and malic enzyme (E. C. 1.1.1.40) were histochemically demonstrated and planimetrically determined. The areas of the enzymes with a maximum activity in the periportal regions, namely SDH and G-6-Pase, were respectively 34% and 41% of the whole parenchyma. Malic enzyme showed a maximum activity in the perivenous region, which consisted of about 53% of the total parenchyma. The zonal distribution of enzyme activities is related only to the terminal vessels; in the vicinity of the preterminal vessels an irregular distribution pattern was found. The results further support the assumption of the bifunctionality of liver parenchyma.
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PMID:[Quantitative investigations of the zonal distribution of SDH, G6Pase and malic enzyme activity in liver parenchyma (author's transl)]. 21 84

The activities of the transmitter metabolizing enzymes monoamineoxidase and acetylcholinesterase and of succinic dehydrogenase were investigated in the telencephalon of Salmo irideus (teleostei). There is a high reaction intensity of the MAO in the whole telencephalon with graded differences between the various nuclear areas. It is highest in the area dorsalis telencephali; the larger fiber tracts (Tr. olfactorius medialis et lateralis; medial and lateral forebrain bundle) are strong MAO-positive, too. There is an extremely weak AchE-reaction throughout the telencephalon. The only nuclear area which is clearly histochemically demonstrable is the regio Dm2 in the area dorsalis telencephali. The SDH-activity is demonstrable in the whole telencephalon. The activity is higher in the area dorsalis as compared with the area ventralis telencephali. In the ependym there are only a few traces of MAO- and SDH-reaction products. The recent findings may support, from a histochemical view, the hypothesis that the telencephalon of Salmo irideus represents brain structures which show structural and functional similarities with limbic telencephalic structures of higher vertebrates.
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PMID:[The activities of the transmitter metabolizing enzymes monoamineoxidase and acetylcholinesterase and of succinic dehydrogenase were investigated in the telencephalon of Salmo irideus (teleostei) (author's transl)]. 30 54

The palatal shelf epithelium of the Mongolian gerbil was examined for succinic dehydrogenase activity prior to, during and the after palatal fusion (days 18-20 post coitus). Enzyme activity was present during all stages examined, and was noted even in the epithelial pearls of fused palates. The presence of SDH activity in these epithelial pearls lends support to the theory 'epithelial stretching', and questions the theory of 'programmed cell death' in relation to the loss of the epithelium along the plane of fusion.
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PMID:Succinic dehydrogenase activity during palate formation in the Mongolian gerbil. 63 9

In a detailed study focused on the methodological problems in dehydrogenase histochemistry [e.g., fixation, diffusion of enzymes and of reduced inermediates, conversion of NADPH and NADP to NADH and NAD, respectively, penetration of tetrazolium salt and formazan substantivity, 'nothing dehydrogenase' reaction, use of exogenous CoQ10 and of flavoprotein substitute (PMS)], the distribution and activity of succinate dehydrogenase, NAD(P)H-tetrazolium reductase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase (H and M types), and of L-glutamate dehydrogenase (E.C.1.4.1.2 and E.C.1.4.1.3) have been investigated in the rat cerebellum. It was evident from the study that reliable results could only be obtained if all the aforementioned factors had been considered. The image of actual concentration of SDH in the neuropil of the molecular layer could only be recorded by adding CoQ10, while other structures exhibited greater balance between SDH and endogenous mitochondrial CoQ. Contrary to previous studies, a reversed localization of the activity of G-6-PDH and LDH was noticed. The elements of molecular and Purkinje layers were rich in G-6-PDH, while the granular layer was nearly depleted. The actual level of LDH could only be recorded if NADH-tetrazolium reductase was bypassed with PMS. The H and M types of LDH coexisted in the three cortical layers, the H type being prevalent and the M type attaining its highest level in synaptic glomeruli followed by the structures of the molecular layer and the Purkinje cells. High activity of GDH was noticed in Bergmann glia followed by synaptic glomeruli, while most other structures showed weak to moderate activity. The two GDH types coexisted in all structures showing activity, except for Bergmann cells, which only showed presence of the E.C. 1.4.1.3 type. Furthermore, Bergmann glia was exceptional by showing no activity of SDH and LDH, but strong activity of G-6-PDH and NADPH-tetrazolium reductase. The granular cells were exceptional by showing weak or no activity of all enzymes in question.
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PMID:Methodological aspects of the histochemical localization and activity of some cerebellar dehydrogenases. 66 87


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