Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.1.1.49 (glucose-6-phosphate dehydrogenase)
 7,794 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myoepithelial and secretory cells from the mammary gland of the lactating rat have been isolated, purified, and characterized. Mammary tissue was dissociated with collagenase into basket-like networks of myoepithelial cells and single secretory cells. Because of their larger size, the myoepithelial cell networks could be separated from other mammary and blood cells by differential centrifugation. Isolated secretory cells were purified by isopycnic centrifugation in 25% bovine serum albumin. The purified myoepithelial and secretory cells were viable, as shown by the incorporation of 32P into distinct macromolecules that were separable by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Both myoepithelial and secretory cells retained their characteristic morphology after isolation and purification, as shown by light, transmission, and scanning electron microscopies. The isolated myoepithelial cells were unique and, thus, distinguishable from other mammary cells in a number of respects; they 1) contracted in response to the addition of oxytocin, 2) bound [3H]oxytocin specifically, 3) accounted for the content of alkaline phosphatase and [Na+ + K+]ATPase in mammary tissue, and 4) reacted specifically with antiserum prepared against purified myoepithelial cells. The purified secretory cells were unique in possessing glucose-6-phosphate dehydrogenase activity. The different cell markers not only gave independent estimates of the purity of the cell fractions, but they also may be helpful in identifying mammary cells in stages of differentiation and neoplastic transformation.
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PMID:Purification and characterization of mammary myoepithelial and secretory cells from the lactating rat. 624 56

Oral administration of manganese chloride (25 mg/kg b. w. daily) to monkeys for a period of 18 months produced congestion and marked increase in weight of testis. Histopathologic examination revealed interstitial oedema and degeneration of seminiferous tubules. Activities of succinic dehydrogenase, glucose-6-phosphate dehydrogenase and acid phosphatase were significantly inhibited whereas NADH-diaphorase and alkaline phosphatase activities showed only slight inhibition in seminiferous tubules of treated monkeys. It was concluded that chronic exposure to manganese does not produce sever degenerative changes in the testis earlier than metal induced encephalopathy in primates.
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PMID:Manganese induced testicular changes in monkeys. 624 33

Oxygen and glucose consumption and lactate production of the peritoneal membrane and intra-abdominal adhesions were measured in rats after a single intra-peritoneal colloidal silica injection. Enzyme histochemical studies were made of lactate dehydrogenase, succinate dehydrogenase, NADH2-diaphorase, NADPH2-diaphorase, glucose-6-phosphate dehydrogenase, glutamate dehydrogenase, acid phosphatase, leucylaminopeptidase and alkaline phosphatase in the peritoneal membrane. Anaerobic glycolysis comprises 47% of the total glucose consumption in the the normal peritoneum. Glucose consumption and lactate production of the peritoneal membrane increased sharply in the early phase of silica-induced peritonitis and stayed at a high level for a week indicating an enhanced anerobic metabolism. Oxygen and aerobic glucose consumption increased more slowly than anaerobic glucose consumption and reached their maxima 1 week after silica injection, indicating that the rate of aerobic metabolism is also higher in chemical peritonitis than in the controls. On the other hand, glucose consumption and lactate production increased in a parallel fashion in adhesions and in the peritoneum in the early phase of peritonitis. However, the maximum and later levels were less in adhesions than in the peritoneum. In the enzyme histochemical study high activities of enzymes indicating anaerobic energy metabolism and metabolism via the pentose phosphate shunt were seen in cells of the peritoneal membrane during the early phase of peritonitis. No activity was identified in enzymes indicating aerobic energy metabolism and increased catabolism before the end of the first week.
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PMID:Energy metabolism of the peritoneal membrane in silica-induced peritonitis. A biochemical and enzyme histochemical study. 625 64

The histochemical enzyme activity of alkaline phosphatase, nonspecific esterase, 5-nucleotidase, beta-glucuronidase, glucose-6-phosphatase, succinate dehydrogenase, and glucose-6-phosphate dehydrogenase in human bladder cancer was investigated. Tumors of 84 patients, classified into grades I-III according to the WHO classification, were compared with 12 normal and 16 inflamed bladder epithelia. As a rule, loss of alkaline phosphatase activity and a decrease of nonspecific esterase activity was found in most of these tumors. The activity of beta-glucuronidase was decreased and compared with normal tissue, also the activity of 5-nucleotidase. The succinate dehydrogenase activity in tumor tissue was frequently increased, whereas glucose-6-phosphate dehydrogenase did not show any significant reaction.
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PMID:[Histochemical investigations on human bladder cancer (author's transl)]. 626 65

The effect of 1-butanesulfonic acid sodium salt and sodium dodecyl sulfate on the activity of highly purified and crystalline enzymes with marked differences in structure and function has been studied. The enzymes were: alcohol dehydrogenase; lactate dehydrogenase; malate dehydrogenase; isocitrate dehydrogenase; glucose-6-phosphate dehydrogenase; lipase; alkaline phosphatase. While 1-butanesulfonic acid sodium salt, at the studied concentrations, resulted generally inactive, sodium dedecyl sulfate showed a selective inhibitory effect, always under the critical micellar concentration. A kinetic analysis of the inhibitory action was also carried out.
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PMID:Specific interaction among some enzymes and sodium dodecyl sulfate. 629 Aug 15

Acute renal failure was induced in rats by injection of a lethal dose of live Escherichia coli. Enzyme activities of the proximal tubule were studied histochemically at three, six, and 12 hours following E coli injection. The enzymes examined were alkaline phosphatase (A1Pase), acid phosphatase (AcPase), adenosine triphosphatase (ATPase), succinate dehydrogenase (SDH), glucose-6-phosphatase (G6Pase), and glucose-6-phosphate dehydrogenase (G6PDH). At three hours, ATPase activity was slightly decreased, while other enzymes showed no changes in activities at this time. At six hours, a slight increase in AcPase activity was seen in the pars recta. At this time, although A1Pase showed no change in activity, other enzymes revealed slight decreases in activities: G6Pase and SDH in the pars convoluta, ATPase in the pars convoluta and pars recta, and G6PDH in pars recta. At 12 hours after treatment, all enzymes showed decreases in activities; however, no necrotic tubule changes were detectable by light microscopy. Since sodium reabsorption in proximal tubules requires a sodium pump consisting of Na-K ATPase, early histochemical changes in ATPase activity in proximal tubule following bacteremia may be related to early changes in sodium reabsorption causing polyuria and to the subsequent development of acute renal failure.
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PMID:The pathophysiology of septic shock: acute renal failure in rats following live E coli injection. A histochemical study of the proximal tubules. 629 45

Young rats were exposed to 2, 5, 8 and 10 Gy 50 kV local irradiation. The epiphyseal region of the proximal tibia was examined with histopathologic, histochemical and enzyme histochemical methods 1 to 90 days after irradiation. One day after irradiation, a decrease in alkaline phosphatase activity was noted and increased activity was found for acid phosphatase, NADH2-diaphorase and glucose-6-phosphate dehydrogenase, especially after 8 and 10 Gy, but also after 5 Gy. Three days after irradiation, all enzymes showed an increased activity and on day 7 the findings resembled those on day 3. Thirty days after irradiation, a return to normal conditions was observed. The most marked morphologic changes were swelling of cells in the hypertrophic cell zone, disturbed order of cells in the zone of proliferation and an increased number of osteoclasts in the metaphyseal bone. These alterations appeared 1 to 3 days after irradiation and normal morphology was seen on day 30 after 2, 5 and 8 Gy and 90 days after irradiation with 10 Gy.
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PMID:Effect of 50 kV irradiation on enzyme activities of growing rat bone. A histopathologic and enzyme histochemical investigation. 630 36

Conditions are described for the preparation of permeabilized cells of Candida albicans. This method has been used for the in situ assay of enzymes in both yeast cells and germ-tube forming cells. A mixture of toluene/ethanol/Triton X-100 (1:4:0.2, by vol.) at 15% (v/v) and 8% (v/v) was optimal for the in situ assay of glucose-6-phosphate dehydrogenase in yeast and germ-tube forming cells, respectively. The concentration of toluene/ethanol/Triton X-100 required for optimal in situ activity of other enzymes was influenced by the cellular location of the enzyme, growth phase and morphology. The membrane-bound enzymes (chitin synthase, glucan synthase, ATPase), cytosolic enzymes (glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, pyruvate kinase, phosphofructokinase, alkaline phosphatase, glucosamine-6-phosphate deaminase and N-acetylglucosamine kinase) and wall enzymes (beta-glucosidase and acid phosphatase) were measured and compared to the activity obtained in cell extracts. The pattern of enzyme induction and the properties of the allosteric enzymes phosphofructokinase and pyruvate kinase were measured in situ. Pyruvate kinase in situ was homotropic for phosphoenolpyruvate with a Hill coefficient of 1.9 and a S0.5 of 0.6 mM, whereas in cell extracts, it had a Hill coefficient of 1.9 and a S0.5 of 1.0 mM. The Km for ATP was 1.6 mM in cell extracts and 1.8 mM in permeabilized cells. In situ phosphofructokinase was homotropic for fructose 6-phosphate (S0.5 of 2.3 mM, Hill coefficient of 4.0). The kinetic properties of pyruvate kinase and phosphofructokinase measured in situ or in vitro were similar for both yeast cells and germ-tube forming cells.
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PMID:The in situ assay of Candida albicans enzymes during yeast growth and germ-tube formation. 631 58

The effects of 1.5 ppm of mercuric chloride (LC50/48 hr) on some enzymes and organic substances of liver tissue of Sarotherodon mossambicus were studied. Significant decreases in the activities of succinate dehydrogenases, lactate dehydrogenases, glucose-6-phosphate dehydrogenase, alkaline phosphatase, and acid phosphatase and in the levels of organic substances like total anthrone-positive substances, glycogen, and total ninhydrin-positive substances were observed. The results indicate impaired oxidative and transphosphorylative activities and utilization of carbohydrates during acute mercury toxicosis in fish.
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PMID:Acute effect of mercury toxicity on some enzymes in liver of teleost Sarotherodon mossambicus. 632 40

In Glossina morsitans morsitans Westwood the locus for glucose-6-phosphate dehydrogenase, G6pd, was found to be in linkage group I, approximately 35 to 42 map units to the left of ocra, the locus for body color. The locus for midgut alkaline phosphatase, Alkph, was found to be in linkage group II, within 0.41 map units of the locus for xanthine oxidase, Xo. The distance from Xo to the locus for aldehyde oxidase, Ao, was confirmed to be about 42 map units. No evidence for genetical recombination was found in male G. m. morsitans.
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PMID:Genetics of Glossina morsitans morsitans (Diptera: Glossinidae). VII. Location of G6pd in linkage group I, and Alkph in linkage group II. 634 Aug 5


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