Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.1.1 (hexokinase)
5,274 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Partial sympathectomy of rat liver, carried out by bilateral section of celiac nerves, caused a distinct increase in the activity of hexokinase and glucose-6-phosphate dehydrogenase and (less distinctly) of 6-phosphogluconate dehydrogenase and lactate dehydrogenase in liver tissue. The alterations in glucokinase activity were not statistically significant. Noradrenaline disappeared completely from rat liver after the celiac nerves section. Activities of the above-mentioned enzymes were altered to the same degree in sympathectomized liver of adrenalectomized animals. The increase in the hexokinase and glucose-6-phosphate dehydrogenase activity was prevented by administration of actinomycin D immediately after the section of celiac nerves. The data obtained suggest that after section of liver celiac nerves the alterations in the enzymatic activities are determined by the increase of their biosynthesis and occur as a result of impairment of liver sympathetic innervation.
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PMID:[Nature of changes in the activity of certain enzymes of energy metabolism in the liver after partial sympathectomy]. 102 52

Soluble enzymes were immobilized and visualized by polyacrylamide gel slabs, impregnated with the incubation medium including auxiliary enzymes. The method has several advantages over existing techniques which make use of gel films or a semipermeable membrane. The diffusion of tissue compounds is effectively limited, while auxiliary enzymes may be operative. Moreover the viscosity of the medium is temperature-independent so that the incubation temperature can be varied. To demonstrate the suitability of the method glycerol-3-phosphate dehydrogenase, lactate dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphoglucomutase and aldolase were visulaized in human or rat skeletal muscle. Cytosolic and mitochondrial glycerol-3-phosphate dehydrogenase were both visualized in the absence of added NAD+ and menadione. For the visualization of ATP producint enzymes, like creatine kinase and pyruvate kinase, the method is not suitable.
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PMID:Polyacrylamide gel technique for the histochemical demonstration of soluble enzymes. 105 94

The activities of glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP oxidoreductase, G6PD), 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase, 6PGD), hexokinase (ATP: D-hexose 6-phosphotransferase, Hx), lactate dehydrogenase (D-lactate: NAD oxidoreductase, LDH). glutamate oxaloacetate transaminase (L-aspartate: 2 oxoglutarate aminotransferase, GOT) and dihydrofolate reductase (DHFR) were measured at 8 a.m. in leucocytes of healthy individuals and patients with chronic myeloid leukaemia (CML), chronic lymphatic leukaemia (CLL), myelofibrosis with myeloid metaplasia and polycythaemia vera. In view of the heterogeneity of the leucocyte populations in these conditions, the enzyme activities were correlated to the number of immature cells in CML and to the percentage of lymphocytes in CLL. No differences in the enzyme activities were found between the white cells of healthy individuals, myelofibrosis with myeloid metaplasia and polycythaemia vera. In CML the activities of all enzymes except GOT correlated directly with the number of immature cells; an inverse correlation with the number of lymphocytes was observed in CLL. GOT was the only enzyme whose activity correlated with the number of lymphocytes in the cell suspension. Furthermore, a significantly higher activity of this enzyme was found in Ficoll-isolated CLL lymphocytes as compared to normal lymphocytes.
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PMID:Blood leucocyte enzymes. II. Activities at 8-9 a.m. in cells of normal subjects, chronic lymphatic leukaemia and chronic myeloid leukaemia patients. 105 70

Enzyme abnormalities are frequently found in the red cells of patients with various acquired blood disorders. In leukaemias, preleukaemic states and bone marrow insufficiencies with or without sideroblastosis, changes in enzyme activity are usually characterized by the coexistence of deficiency of some enzymes and an increased activity of others. The most frequently decreased activities are those of pyruvate kinase, phosphofructokinase,2,3-diphosphoglycerate mutase and adenylate kinase; the most frequently increased activities are those of hexokinase, aldolase, enolase, 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase. In primary myelofibrosis and in polycythaemia rubra vera, enzyme deficiencies are infrequent and differ from those observed in leukaemias and related disorders. Phosphohexose isomerase and phosphoglucomutase deficiencies seem relatively specific for polycythaemia rubra vera. Explanations for the acquired enzymopathies are still at the stage of hypothesis. The theory of multiple genetic damage may explain some findings but has not yet been proved right. The possibility of post-translational molecular modification is suggested as a working hypothesis.
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PMID:Acquired erythroenzymopathies in blood disorders: study of 200 cases. 107 44

Histologic investigations together with histochemical and photometric measurements of enzyme activities were performed in retina of rabbits, whose blood supply had been totally interrupted for 1h. A retinal edema developed affecting the internal layers between the inner limiting membrane and the internal plexiform and ganglion cell layer. Although this edema was quite remarkable at the posterior pole of the eye, it diminished toward the periphery, disappearing near the ora serrata. The activities of the following enzymes were investigated: hexokinase, glucose 6-phosphate dehydrogenase, aldolase, glyceraldehydephosphate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, ATPase, and phosphorylase. The most striking finding was the total disappearance of phosphorylase activity under pressure ischemia. ATPase and aldolase showed a decreased activity in the ischemic retina, and malate dehydrogenase a slightly diminished one. Concerning the other enzymes, no significant differences between normal and ischemic retina were observed.
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PMID:Enzymologic and histologic investigations in normal and pressure-ischemic retina of rabbits. 108 79

Nitrogen mustard (NH2) and Nor-nitrogen mustard (Nor-HN2) both inhibit the polymerization of deoxyhemoglobin S in solution and in intact erythrocytes. Metabolic studies were undertaken to determine the feasability of an extracorporeal treatment with these or related agents. Glucose utilization, hexose monophosphate shunt activity, methemoglobin reduction, and incubation with acetylphenylhydrazine for Heinz body formation were performed, as well as specific assays for hexokinase, pyruvate kinase, glucose-6-phosphate dehydrogenase, glutathione reductase, ATP, reduced glutathione (GSH), and survival of autologous mustard-treated cells in rabbits. HN2 was found to enter red cells rapidly and bind to intracellular contents. Metabolic studies revealed no significant inhibition or alteration of function by Nor-HN2 at 10 mg/ml of whole blood. Rabbit red cell survival was also normal. HN2, however, inhibited glutathione reductase and blocked the free sulfhydryl group of GSH by forming serveral addition products of alkylated GSH. Heinz body test with acetylphenylhydrazine became positive in HN2-treated cells, and rabbit red cell survival was shortened considerably in the concentration range used to inhibit sickling. Ascorbic acid stimulation of the hexose shunt pathway was inhibited by HN2, but methylene blue stimulation remained unaffected. 14-C-HN2 remains bound to red cells in vivo, and the disappearance of radioactivity is similar to that found with 14-C-DFP (disopropylfluorophosphate). Oxygen affinity of both HN2 and Nor-HN2 treated human red cells remains virtually the same as that found in control samples. It is concluded that Nor-HN2 may be a suitable agent for an extracorporeal therapy, and that each mustard needs to be evaluated individually for its antisickling effects and its suitability for extracorporeal use.
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PMID:Metabolic effects of antisickling amounts of nitrogen and nor-nitrogen mustard on rabbit and human erythrocytes. 112 27

Sodium fluoride was inadvertently added as a preservative to the urine of an eight-year-old boy with diabetes mellitus before urinary glucose was measured. On preliminary screening of the urine, the test by glucose oxidase paper reagent strip gave a negative reading for glucose, whereas quantitative urinary glucose assay by the coupled enzyme reaction (hexokinase-glucose 6-phosphate dehydrogenase) gave a glucose concentration of 81.5 g/liter. Inadvertent use of sodium fluoride as a urine preservative may cause a falsely negative result with the glucose tests involving oxidase.
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PMID:Inhibitory effect of fluoride on glucose tests with glucose oxidase strips. 113 42

Triethyloxonium tetrafluoroborate was used to O-alkylate nylon-tube thus producing the imidate salt of the nylon which was further made to react with 1,6-diaminohexane. 2. Hexokinase (EC 2.7.1.1) and glucose 6-phosphate dehydrogenase (EC 1.1.1.49) were immobilized on the amino-substituted nylon tube through glutaraldeyde and bisimidates. 3. The effect of varying the conditions of O-alkylation and the amount of enzyme immobilized on the activity of nylon tube-hexokinase derivatives was determined. 4. The effect of varying the amount of enzyme immobilized on the activity of nylon-tube-glucose 6-phosphate dehydrogenase derivatives was determined. 5. The thermal stability of nylon-tube-hexokinase and nylon-tube-glucose 6-phosphate dehydrogenase derivatives was studied. 6. Different ratios of hexokinase and glucose 6-phosphate dehydrogenase were co-immobilized on nylon tube, and the rate of conversion of glucose into 6-phosphogluconolactone was compared with the individual activities of the immobilized enzymes. 7. Hexokinase and glucose 6-phosphate dehydrogenase co-immobilized on nylon tube were used in the automated analysis of glucose.
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PMID:The preparation of nylon-tube-supported hexokinase and glucose 6-phosphate dehydrogenase and the use of the co-immobilized enzymes in the automated determination of glucose. 116 61

Enzyme activities operative in glucose degradation and citrate cleavage pathway were studied in the adipose tissue of twenty-four patients with adult-onset diabetes and normal body weight, aged 59+/-9 years, and twenty-four matched controls. In normal tissue, type II (heat-inactivated) hexokinase moderately predominated over type I (heat-resistant). 6-Phosphofructokinase had an extremely low activity, which was by far the lowest among the ten glycolytic enzyme activities investigated, and which therefore might greatly limit the glycolytic rate. The level of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating) was elevated above that occurring in other tissues. This, especially if considered together with the low 6-phosphofructokinase activity, would suggest a major role of pentose cycle in glucose degradation. Of the citrate cleavage pathway enzymes, ATP citrate-lyase, although having a lower activity than malate dehydrogenase and malate dehydrogenase (decarboxylating) (NADP), was readily measurable, which contrasts with previous data by others. This finding is consistent with the occurrence of lipogenetic capacity in human adipose tissue. In diabetic tissue, there was a decreased activity, both on a protein and on a wet-weight basis, of enzymes concerned with the glucose entry into metabolic pathways, namely hexokinase (both type I and, especially, type II) and pentose cycle dehydrogenases, as well as of pyruvate kinase. This could be connected with the defective glucose utilization by adipose tissue in diabetes. Beside the above-mentioned dehydrogenases, malate dehydrogenase (decarboxylating) (NADP) was also diminished. The reduction of these NADPH-forming enzymes, which supply reducing equivalents for fatty acid synthesis, would suggest a depressed lipogenesis.
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PMID:Enzymes of glucose metabolism and of the citrate cleavage pathway in adipose tissue of normal and diabetic subjects. 118 27

The realtionship between growth rate and the metabolic activity of certain liver enzymes was studied using two strains of White Plymouth Rock chickens which had been selected in divergent directions for eight-week body weight. The activities of hexokinase, glucokinase, phosphofructokinase, glucose-6-phosphate dehydrogenase, citrate synthase, glycogen synthetase, glutamate dehydrogenase and aspartate transaminase were measured at 4, 8 and 20 weeks of age. The mean percentage rate of growth of the birds selected for high eight-week body weight exceeded that of the birds selected for low eight-week body weight only during the early growth period. Thereafter, and until sexual maturity, the low-line birds grew at a faster rate, relative to body size. The mature body weight of the high-line birds exceeded that of the low-line birds by a factor of approximately 1.5. A close similarity was noted between the metabolic activity of certain liver enzymes and the growth rate (relative to body size) of the birds studied. At four and eight weeks of age, the faster-growing birds (whether high- or low-line) generally exhibited a greater capacity for glucose phosphorylation and glycolysis, but a poorer capacity for glycogen synthesis, than the slower-growing birds. At twenty weeks, growth rate and metabolic activity were similar in both strains.
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PMID:Activity of certain liver enzymes in fast- and slow-growing lines of chickens. 118 17


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