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)

(1) The histochemical staining pattern of succinic dehydrogenase (SDH) does not show unequivocal differentiation between the type I red and type II red fibres in mammalian striated muscles. (2) Since high biochemical activity of beta-hydroxybutyric dehydrogenase (beta-HOBDH) occurs in mitochondria of the type I red fibres, the histochemical localization of this enzyme may show a pattern of staining reciprocal to that seen for myofibrillar ATPase. (3) It remains to be confirmed that the type I red fibres, which are possibly slow-twitch physiologically, possess the highest concentration of myoglobin. The histochemical correlation of myoglobin and myofibrillar ATPase in serial sections should be studied. (4) In order to achieve a more realistic picture, various glycolytic and glycogenolytic enzymes should be incubated according to the gelatin film technique, or semipermeable membrane technique or collagen polypeptide technique. A histochemical correlation of phosphorylase, LDH, PFK, alpha-glycerophosphate dehydrogenase, and myofibrillar ATPase in adjacent muscle sections may throw light on the histochemical characteristics of the different fibre-types. (5) The specific histochemical demonstration of AMPase is achieved following preincubation of tissue sections. (6) ADPase has been demonstrated by the calcium precipitation technique only (GUTH and YELLIN, 1971). A number of studies claim, however, that ADPase is not demonstrable histochemically in muscle fibres. (7) The presence of magnesium ions is a prerequisite for the adequate histochemical demonstration of mitochondrial ATPase. The latter is inhibited almost completely by 40 mM Ca++ (when Mg++ is not added) at both neutral and alkaline pH values. (8) The histochemical activity of SR-AT-Pase seen as continuous reticula but without punctuate and sub-sarcolemmal staining possibly represents the extra ATPase of SR. (9) On the basis of myofibrillar ATPase reaction, an inherent heterogeneity, between the type II red and type II white may be recognized. In addition, the above fibre-types possess their respective sub-populations. (10) Following diK+ EDTA preincubation, some type II red fibres show selective lability. These are the mitochondria-rich fibres. Thus in the total absence of both punctuate and subsarcolemmal staining, the presence of mitochondrial ATPase activity under the histochemical conditions for myofibrillar ATPase is unlikely. (11) The reaction pattern of CK/ATPase (coupled reaction) at pH 6.9 is distinctly intermyofibrillar and unlike SDH-pattern. This reticular reaction is associated mainly with the SR and hence the importance of transphosphorylation in this organelle for the Ca++ uptake and muscle relaxation. (12) The CK/ATPase reaction at pH8.0 has shown important histoenzymatic characteristics. At this pH value the type I red fibres and slow-twitch soleus show myofibrillar reaction pattern. This identical histochemical behaviour suggests that type I red fibres are possibly slow-contracting...
 ...
PMID:Histochemical characteristics of vertebrate striated muscle: a review. 18 61

Aging has recently been shown to promote lipid peroxidation of mitochondrial membranes by a mechanism involving chaotropic oxidants (5). The present paper reports on the relationship between these membrane alterations and the activities of lipid-dependent enzymes of isolated heart mitochondria from 3 month and 24 month old rats. 1. Temperature breaks of Arrhenius plots reveal age-dependent shifts to higher temperatures for the succinate oxidase system (delta t = 1,7 degrees C), the beta-hydroxybutyrate dehydrogenase, the succinate dehydrogenase and the ATP-ase (delta t = 3,0 degrees C). 2. Specific activities of the above enzymes are distinctly lowered in preparation from aged rats. 3. Thermotropic differences of the particular enzyme activities completely disappeared after solubilization of the lipid components by Triton X-100. 4. ESR studies exhibit a clear decrease in the fluidity of membrane lipids as a function of age. 5. Analysis of the membrane lipids by gas-liquid chromatography reveals a distinct age-dependent fall in the content of polyunsaturated fatty acids accompanied by a slow increase in the degree of fatty acid saturation. 6. It is concluded from the results that aging influences enzyme-protein-lipid interactions by radical-induced peroxidation of the surrounding membrane lipids, but does not affect the intrinsic properties of the membrane-bound enzymes themselves.
 ...
PMID:Influence of age on thermotropic kinetics of enzymes involved in mitochondrial energy-metabolism. 21 32

The segmentation of the proximal tubules in the kidney of the female rat was studied by means of enzyme histochemical reactions and the results compared with those observed in male and recently described by Jacobsen and J0rgensen (1973 a). Reactions were performed for the following soluble, coezyme-dependent oxido-reductases: glucose 6-phosphate dehydrogenase, alpha-glycerophosphate dehydrogenase, 3 alpha-hydroxysteroid dehydrogenase, NAD-as well as NADP-dependent isocitrate dehydrogenases, NAD-dependent malate dehydrogenase, NADP-dependent, decarboxylating malate dehydrogenase, uridine diphosphate glucose dehydrogenase. Measures were taken to reduce enzyme diffusion and eliminate interference from tissue tetrazolium reductases. Furthermore, reactions were performed for a number of less soluble or insoluble enzymes: glucose 6-phosphatase, mitochondrial alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, succinate dehydrogenase and tetrazolium reductases. In the proximal tubules of the female rat all enzymes studied--except beta-hydroxybutyrate dehydrogenase--showed segmental differences, most of them clearly revealing three segments. Sex differences were found concerning all enzymes except uridine diphosphate glucose dehydrogenase and NADP-dependent isocitrate dehydrogenase. The most pronounced sex-related differences were seen in the third segment in which part the male rat showed highest activity in respect to tetrazolium reductases, NAD-dependent isocitrate dehydrogenase, succinate dehydrogenase, beta-hydroxybutyrate dehydrogenase, 3 alpha-hydroxysteroid dehydrogenase and glucose 6-phosphate dehydrogenase and the female in respect to glucose 6-phosphatase, alpha-glycerophosphate dehydrogenases, and NADP-dependent, decarboxylating malate dehydrogenase. A few of the enzymes exhibited minor sex differences in the first two segments.
 ...
PMID:Enzyme histochemical observations on the segmentation of the proximal tubules in the kidney of the female rat. 23 55

1. Enzyme activities (units/g wet wt.) were determined in the caput and cauda epididymidis and in epididymal spermatozoa of the rat. 2. The activity of most enzymes in the cauda was between 50 and 100% of that in the caput, except that ATP citrate lyase was barely detectable in the cauda. 3. Spermatozoa, unlike epididymal tissue, contained sorbitol dehydrogenase but lacked ATP citrate lyase. NADP+-malate dehydrogenase, mitochondrial glycerol 3-phosphate dehydrogenase, succinate dehydrogenase, carnitine acetyltransferase and citrate synthase were 5 to 400 times as active in spermatozoa as in epididymal tissue. 4. 2-Oxoglutarate dehydrogenase was the least active member of the tricarboxylic acid cycle in all tissues and most closely matched the measured flux through the cycle. 5. The concentrations of hydroxyacyl-CoA dehydrogenase and carnitine palmitoyltransferase were equivalent to the more active enzymes of the tricarboxylic acid cycle, indicating the capacity for extensive lipid oxidation, and the presence of 3-hydroxybutyrate dehydrogenase suggests that these tissues can also oxidize ketone bodies. 6. Transfer of reducing equivalents from cytoplasm to mitochondrion is unlikely to occur by means of the glycerol phosphate cycle because mitochondrial glycerol 3-phosphate dehydrogenase is relatively inactive in epididymal tissue, whereas the cytoplasmic enzyme has little activity in spermatozoa, but transfer may be accomplished by the malate-aspartate shuttle. 7. Transfer of acetyl units from mitochondrion to cytoplasm could be effected by the pyruvate-malate cycle in the caput of androgen-maintained rats, but not in the other tissues because of the low activity of ATP citrate lyase. Acetyl unit transfer could take place via acetylcarnitine, mediated by carnitine acetyltransferase. 8. Castration resulted in a decrease in the concentration of nearly all enzymes, although subsequent administration of testosterone restored concentrations to values similar to those in animals maintained by endogenous androgen. The extent to which enzyme concentration was changed by an alteration in androgen status was highly variable, but was most marked in the case of pyruvate carboxylase.
 ...
PMID:Activity and androgenic control of enzymes associated with the tricarboxylic acid cycle, lipid oxidation and mitochondrial shuttles in the epididymis and epididymal spermatozoa of the rat. 72 83

By means of histochemical methods (gel-film incubation-media) superficial spreading melanoma, nodular melanoma and lentigo maligna melanoma are investigated. The result of this examination is that with regard to their enzyme spectra, the nodular melanoma and the nodular part of the superficial spreading melanoma are very similar. Glucose-6-phosphate dehydrogenase shows the strongest enzyme reaction, followed by succinate dehydrogenase and lactate dehydrogenase. The beta-hydroxybutyrate dehydrogenase reaction is always weak. The reaction of acid phosphatase is between negative and weakly positive. Significant differences, however, are observed in lentigo maligna and in lentigo maligna melanoma. In both, the strongest formazan deposits are seen with succinate dehydrogenase, sometimes also with lactate dehydrogenase. The glucose-6-phosphate dehydrogenase reaction, however, is sometimes considerably weaker. In the case of lentigo maligna melanoma, the activity of beta-hydroxybutyrate dehydrogenase often is increased, and acid phosphatase also shows higher reactions than in the other melanomas. These differences in the enzyme pattern correspond to the different biological behavior of the tumours. The enzymatical and biological characteristics of lentigo maligna melanoma possibly derive more from the characteristics of the tumour itself which are not dependent on the area.
 ...
PMID:Histochemical findings in different types of malignant melanoma: biological and clinical significance. 81 58

In the paper we observed histochemically the distribution and activity of 16 enzymes in the normal rat gastric mucosa. The lysosomal enzymes were demonstrated by the method of semipermeable membranes (LOJDA 1972). At the proof of dehydrogenases aqueous and gel media were used. The parietal cells of the gastric mucosa contained a moderate activity of acid phosphatase, E-600 resistant esterase, and only a very slight activity of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase. The macrophages of the interstice contained a high activity of beta-glucruonidase, acid phosphatase, E-600 resistant esterase and a low activity of N-acetyl-beta-D-glucosaminidase. The chief cells of the rat gastric mucosa, in contrast to the human, did not contain nonspecific esterase and also in them acid phosphatase was mostly lacking. The alkaline phosphatase was found only in the endothelium of the capillaries of the gastric mucosa. The parietal cells contained high activities of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, NADH tetrazolium reductase, a lower activity of NADPH tetrazolium reductase, as well as other soluable dehydrogenases. At the examination of dehydrogenases using aqueous as well as gel media with PMS during optimal short incubation periods, we found more and less active forms of parietal cells. The different oxidoreductase capacity of parietal cells in normal rat gastric mucosa can point to their unequal-functional load at the production of hydrochloric acid. The findings obtained are compared with the findings in older papers concerning different experimental animals and with the distribution of enzymes in the human gastric mucosa.
 ...
PMID:Histochemical localization of enzymes in the normal rat gastric mucosa using the technique of the semipermeable membranes and the other methods. 82 7

The myoepithelium of developing, lactating, and involuting mammary gland of the mouse exhibits a high alkaline phosphatase activity. The content of the alveoli and the apical plasma membrane of gland cells histochemically show enzyme activity before and after lactation but not during milk secretion. In the course of involution the alveoli shrink in size and the reaction of alkaline phosphatase becomes stronger in the gland tissue. In whole breast tissue the enzyme activity decreases, because in this time a great part of the alveoli are degraded and replaced by connective tissue and fat. As measured by a scanning microdensitometer the activity of some oxydoreductases (3-hydroxybutyrate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, and succinate dehydrogenase) increase in proceeding development of the mammary gland and reach their highest level at the time of lactation. Already 12 h after the start of involution the oxydoreductases loose 30 to 50% of their activity and undergo a further reduction 3 to 4 days later. On the other side the activity of lysosomal enzymes increase during involution. beta-Glucuronidase and leucine aminopeptidase have their highest activity in the early stage of involution, whereas acid phosphatase predominate in the late period of gland degradation.
 ...
PMID:[Microdensitometric measurement enzyme activities in the mammary gland of the mouse]. 83 21

The subcellular distribution of mitochondrial enzymes was studied in cerebral hemispheres of 15-day-old and adult rats. At both ages the synaptosomal fraction contained very little glutamate dehydrogenase (EC 1.4.1.2) but significant amounts of succinate dehydrogenase (EC 1.3.99.1), glutaminase (EC 3.5.1.2), hexokinase (EC 2.7.1.1), malate NADP dehydrogenase (EC 1.1.1.40) and beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30). In immature brain, in the fraction enriched with free (perikaryal) mitochondria, the concentrations of these enzymes were 9.5, 1.8, 2.0, 0.92, 1.5, and 2.1 times higher, respectively, than in the synaptosomes. The increase with age in succinate dehydrogenase and glutaminase was restricted to free mitochondria while hexokinase and malate NADP dehydrogenase accumulated and beta-hydroxybutyrate dehydrogenase diminished in both fractions. In adult brain, too, where the above ratios became 7.5, 5.2, 3.5, 0.84, 1.4, and 2.0, respectively, the concentrations of enzymes relative to each other distinguished clearly between free and synaptic mitochondria. The results substantiate previously noted signs of mitochondrial heteroeneity in adult brain, and extend them to immature brain. The chemical composition, the quantitative pattern of enzymes, of free and synaptic mitochondria is clearly different, and undergoes separate changes during postnatal differentiation.
 ...
PMID:Distribution of mitochondrial enzymes between the perikaryal and synaptic fractions of immature and adult rat brain. 83 6

A chromatolysis study, 14 to 21 days following denervation, showed the spinal cord representation of the nerve to the posterior latissimus dorsi muscle to be in the ventrolateral cell column between cervical ganglia 14 and 15. to characterize cevical neruos nt undergoing chromatolysis, histochemical stuies were done the cords of additional nondenervated animals. Staining reactions for beta-hydrocybutyrate dehydrogenase, succinic dehydrogenase and cholinesterase did not reveal any quantitative differences between motor neurons in cervical segments 14 and 15 of normal and dystrophic birds. Motor neurons are positive for beta-hydroxybutyrate dehydrogenase and succinic dehydrogenase, but the surrounding neuropil is positive for the latter only. No pseudocholinesterase activity is found in the ventral horn cells, but true cholinesterase is present in most of the neurons...
 ...
PMID:A histochemical study of cervical motor neurons and the posterior latissimus dorsi muscle in normal and dystropic chickens. 120 10

When cervical segments 14 to 15 of the chicken spinal cord are cut transversely and studied by routine histological and histochemical methods, an onion-shaped region, filled with thread-like fibers, is seen to surround the ependymal cells of the central canal and to be bounded laterally by the neural elements of the spinal gray matter. This area is negative for succinic dehydrogenase, beta-hydroxybutyrate dehydrogenase and cholinesterase activity, but very strongly periodic acid-Schiff positive. Diastase controls show the positive material to be glycogen. Parasagittal sections through this cervical region and into the upper thoracic cord, show the glycogen-rich region to extend longitudinally throughout the region. Because of its location and histochemical characterization, which are similar to that of the ventral portion of the glycogen body, the term brachial glycogen body is proposed for this structure.
 ...
PMID:A brachial glycogen body in the spinal cord of the domestic chicken. 124 79


1 2 3 4 5 Next >>