Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.37 (malate dehydrogenase)
4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Repeated injections of rat with 1-thyroxine (50 microgram/kg daily for 5 five-day weeks) retarded the weight gain of the animals and increased the absolute and relative size of the heart, adrenals and interscapular brown adipose tissue. In the myocardium and thigh muscle, thyroxine treatment resulted in elevated activity of oxidative enzymes, succinate dehydrogenase, malate dehydrogenase and citrate synthase, while the activities of glycolytic enzymes remained unchanged. Glycogen content of the heart was decreased following thyroxine regime. In the brown fat, on the other hand, thyroxine injections resulted in a reduction of the activity of oxidative enzymes. This reduction can be accounted for by the decreased protein (enzyme) content of the tissue due to deposition of fat. Furthermore, thyroxine treatment delayed the body cooling of the rats swimming in water at 25 degrees C and enhanced hyperthermic response to injected noradrenaline. All these changes, which were not observable in rats treated with daily alprenolol (20 mg/kg) injections, were as pronounced in rats injected with alprenolol together with thyroxine as in rats injected with thyroxine only. It is concluded that beta blockers do not antagonize the metabolic changes due to hyperthyroidism.
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PMID:Alprenolol fails to antagonize the metabolic changes following repeated thyroxine injections in the rat. 2 61

The metabolic effects on rat cardiac and skeletal muscle of a strenous program of swimming, of cold acclimation and of isoprenaline treatment (0.3 mg/kg daily for 5 five-day weeks) were compared. Exercised and cold-exposed rats gained less body weight than did controls or isoprenaline-treated rats. In all treated groups the heart and the intercapular brown adipose tissue hypertrophied. The size of the adrenals increased only in isoprenaline-treated animals. Cold-acclimation and physical training increased and isoprenaline treatment reduced or did not affect the activities of succinate dehydrogenase, malate dehydrogenase and citrate synthase of cardiac muscle. In the skeletal muscle all treatments resulted in increased activities of these enzymes. Of the anaerobic enzymes analysed, only the activity of hexokinase increased in response to the treatements used. This increase was the same in cardiac as in skeletal muscle, but it was significantly greater with isoprenaline-treatment than with training or with cold-acclimation. The activities of lactate dehydrogenase and phosphofructokinase did not differ significantly. All treatments improved cold resistance, but only swimming exercise and cold acclimation significantly increased tolerance to exercise. It is concluded that prolonged stimulation of adrenergic beta-receptors by catecholamines is responsible for the metabolic changes observed.
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PMID:Comparison of the effects of physical exercise, cold acclimation and repeated injections of isoprenaline on rat muscle enzymes. 12 87

The activity of certain enzymes of energy metabolism (cytochrome c oxidase, citrate synthase, malate dehydrogenase, and lactate dehydrogenase) and of lysosomes (beta-glucuronidase, beta-N-acetylglucosamindase, arylsuphatase, ribonuclease, deoxyribonuclease, acid phosphatase, and cathepsin D) was assayed from m. rectus femoris of mice trained 5 days per week, 1 hr per day for 4 weeks according to 4 different programmes: I. running speed 20 m/min, horizontal track, II. 25 m/min, horizontal track, III. 20 m/min 8 degrees uphill inclination, and IV. 25 m/min 8 degrees uphill inclination. Oxidative capacity increased and anaerobic capacity decreased without distinction between the different traning programmes. Of acid hydrolases assayed the activities of beta-glucuronidase and cathepsin D were increased independently of training intensity. Simultaneous histochemical observations on beta-glucuronidase and arylsulphatase activities in the contralateral m. rectus femoris showed more intense staining in red as compared to white muscle fibres. It is suggested that training affected the red fibres and that the applied level of loading was probably too low to cause major involvement of white fibres.
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PMID:Oxidative and lysosomal capacity in skeletal muscle of mice after endurance training of different intensities. 21 99

Typical metabolic patterns are detectable in the livers of growing rats after feeding diets with high (25%) or low (2%) fat contents. In view of the elucidation of problems related to the regulation of the metabolic processes, it is of interest to know in what way these metabolic patterns change after short-time change from the one diet to the other and if there are hierarchies. Within 2 days after change of diet, the enzymes glucose-6-phosphate dehydrogenase, NAD-malate dehydrogenase, lactate dehydrogenase, citrate synthase and fatty acid synthase were affected, only the 3'.5'-c AMP-splitting phosphodieterase showed no change. The metabolites lactate and pyruvate also changed, inversely to lactate dehydrogenase activity, the lactate-pyruvate ratio remaining almost constant. Acetyl CoA also responded in a characteristic manner. The single parameters were differently affected by the kind of the change of diet (from high-fat to low-fat diet or inversely). For example, glucose-6-phosphate dehydrogenase responded very rapidly to the change from the high-fat to the low-fat diet, malate dehydrogenase behaved inversely, and citrate synthase responded to both changes. Consequently, the regulatory processes after change of diet start from different sides. It is thinkable that this behaviour is related to the different roles of the determined parameters in fat and energy metabolism.
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PMID:[Behavior of certain parameters of lipid and energy metabolism. 5. Effects of high-fat and low-fat diets on certain biochemical parameters in rat livers before and after change of diet]. 21 48

The changes induced by phenobarbital in cerebral enzymatic activities of the Krebs' cycle (citrate synthase, malate dehydrogenase) and electron transfer chain (total NADH-cytochrome c reductase and cytochrome oxidase) were studied. In addition, the activity of lactate dehydrogenase of acetylcholine esterase and of glutamate dehydrogenase was also studied. These enzymatic activities were evaluated in the homogenate in toto and in a crude mitochondrial fraction from rat brain. The modifications in some of these activities indicate that several new metabolic situations occur in brain tissue after phenobarbital treatment.
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PMID:Effect of phenobarbital on cerebral energy state and metabolism. Enzymatic activities. 23 Jun 18

1) Albumins and globulins were prepared from dry seeds of cucumbers (Cucumis sativus) by differential extraction. The globulin fraction was analyzed by gel electrophoresis under denaturing conditions in the presence and absence of mercaptoethanol. The subunit (Mr = 54000) of the tetramer (Mr = 240000) was shown to be composed of two different peptides. Microheterogeneity rendered the exact interpretation of the analysis difficult. 2) Glyoxysomal proteins were already present in dry seeds: malate synthase, isocitrate lyase, citrate synthase, malate dehydrogenase, catalase and crotonase could be detected unequivocally. It was demonstrated that the enzymatic and immunological properties of malate synthase and isocitrate lyase were not distinguishable from that of enzymes assigned to glyoxysomes of fully developed cotyledons. 3) Homogenates prepared from seeds by cautious cell disintegration were subjected to sucrose density gradient centrifugation and yielded microbody and protein body fractions, among other things.
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PMID:Albumins, glyoxysomal enzymes and globulins in dry seeds of cucumis sativus: qualitative and quantitative analysis. 42 26

1. The changes with the time of the activities of some energy-supplying enzymes and of the hydrolytic enzyme, acid phosphatase, were studied over 2 weeks of complete ischaemia, produced in the rat soleus muscle by section of the abdominal aorta and terminal devascularization, leaving nerve and tendon intact. 2. Activities of glycolytic enzymes, oxidative enzymes, hexokinase and acid phosphatase are affected in a different manner. Activities of the glycolytic enzymes, lactate dehydrogenase, triosephosphate dehydrogenase and glycerolphosphate dehydrogenase, are lowest on the 1st day and increase thereafter. The first two reach the control values again on the 4th and 14th day, respectively, while glycerolphosphate dehydrogenase reaches about 50% of the control value on the 14th day. The maximum decrease in activity of the oxidative enzymes, citrate synthase, beta-hydroxyacyl-CoA-dehydrogenase and malate dehydrogenase occurs later (4th day); thereafter their activity returns slowly to control values, but does not reach them even on the 14th day. Hexokinase activity is slightly decreased on the 1st day; then it increased and reached on the 7th day twice the control value. Thus on the 1st day the activity of the enzymes of aerobic metabolism prevail, and on the 4th day those of anaerobic carbohydrate (glucose) metabolism; the recovery of enzyme activity of aerobic oxidation occurs later. 3. Acid phosphatase activity increased from the 2nd day onwards, reaching up to 3 times the control value on the 4th day and still twice that value on the 14th day. This agrees well with the histochemical picture of acid phosphatase. 4. Histochemical changes of alkaline phosphatase activity reveal destruction of capillary endothelial cells during the first few days after operation and their later proliferation from the periphery, correlating with the loss and recovery of oxidative enzyme activity.
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PMID:Effects of ischaemia on enzyme-activities in the soleus muscle of the rat. 57 Nov 16

Soluble bifunctional enzyme aggregates have been prepared by cross-linking the sequential enzymes malate dehydrogenase (EC 1.1.1.37) and citrate synthase (EC 4.1.3.7) using glutaraldehyde. The kinetic behaviour of this two-enzyme system in its aggregated and non-aggregated form was studied both in free solution and immobilized on Sepharose beads. This study was undertaken in order to distinguish between the following two factors which may account for the increased efficiency found in general in co-immobilized consecutive two-enzyme systems: (a) closer proximity between the participating enzymes and (b) establishment of a favourable microenvironment (such as higher local intermediate concentration caused by increased diffusional hindrance in the gel phase). It was found that in spite of a reduction of the distance between the two enzymes in the aggregated form by an estimated factor of 10(3), no kinetic advantage (shorter lag phase or higher steady-state rate) could be detected compared to the corresponding system with the two enzymes not linked to each other. However, both systems immobilized to Sepharose reached the steady-state rate of citrate formation almost immediately, in contrast to the corresponding free systems which exhibited pronounced lag phase. These results indicate that, at least in the above systems and under the conditions given, diffusional hindrance in the gel phase of the intermediate oxaloacetate, which is present in rate-limiting concentrations, is the dominant cause of the observed higher efficiency in immobilized systems.
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PMID:Aspects of microenvironmental compartmentation. An evaluation of the influence of restricted diffusion, exclusion effects, and enzyme proximity on the overall efficiency of the sequential two-enzyme system malate dehydrogenase--citrate synthase in its soluble and immobilized form. 59 Feb 71

Rats were treated by daily alprenolol (10, 20 and 50 mg/kg) injections for 5 days a week for 4 weeks. At 20--21 degrees C alprenolol treatment retarded the weight gain of the animals and increased the weight of the adrenals. These changes were not seen at 29 degrees C. The reduction in size and fat content of the interscapular brovin adipose tissue in drug-treated rats was independent of experimental temperature. At 20--21 degrees C prolonged beta-blockade did not cause any changes in the enzymes of the energy metabolism. At 29 degrees C, however, alprenolol treatment antagonized the decrease in activity of oxidative enzymes (succinate dehydrogenase, malate dehydrogenase, citrate synthase) and the decrease in protein concentration of the cardiac muscle. In skeletal muscle alprenolol treatment significantly decreased the activities of oxidative enzymes and antagonized the rise in the activity of lactate dehydrogenase resulting from warm acclimation. The increased activities of oxidative enzymes in interscapular brown adipose tissue of aprenolol treated rats were coupled with an increase in protein concentration of the tissue. Although these changes were more marked at 29 degree C they were observable at 20--21 degree C, too. The difference in the drug effects at 20--21 degrees C and 29 degrees C can be accounted for by the compensatory catecholamine release at the lower temperature, due to impaired thermoregulatory capacity after alprenolol. Prolonged beta blockade decreased the exercise tolerance and cold tolerance of the rats. An increased response of the diastolic blood pressure to an alpha-adrenergic drug, noradrenaline, and a decreased response to a beta-adrenergic drug, isoprenaline, in alprenolol-treated rats indicates a shift from beta- to alpha-receptors.
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PMID:Effect of prolonged beta-blockade on energy metabolism and adrenergic responses in the rat. 59 3

The pathway of acetate assimilation in Methanosarcina barkeri was determined from analysis of the position of label in alanine, aspartate, and glutamate formed in cells grown in the presence of [14C]acetate and by measurement of enzyme activities in cell extracts. The specific radioactivity of glutamate from cells grown on [1-14C]- or [2-14C]acetate was approximately twice that of aspartate. The methyl and carboxyl carbons of acetate were incorporated into aspartate and glutamate to similar extents. Degradation studies revealed that acetate was not significantly incorporated into the C1 of alanine, C1 or C4 of aspartate, or C1 of glutamate. The C5 of glutamate, however, was partially derived from the carboxyl carbon of acetate. Cell extracts were found to contain the following enzyme activities, in nanomoles per minute per milligram of protein at 37 degrees C: F420-linked pyruvate synthase, 170; citrate synthase, 0.7; aconitase, 55; oxidized nicotinamide adenine dinucleotide phosphate-linked isocitrate dehydrogenase, 75; and oxidized nicotinamide adenine dinucleotide-linked malate dehydrogenase, 76. The results indicate that M. barkeri assimilates acetate into alanine and aspartate via pyruvate and oxaloacetate and into glutamate via citrate, isocitrate, and alpha-ketoglutarate. The data reveal differences in the metabolism of M. barkeri and Methanobacterium thermoautotrophicum and similarities in the assimilation of acetate between M. barkeri and other anaerobic bacteria, such as Clostridium kluyveri.
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PMID:Acetate assimilation pathway of Methanosarcina barkeri. 76 16


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