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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)

The mitochondrias of the hyalocytes contain lactic dehydrogenase but no glucose-6-phosphate dehydrogenase, so that only aerobic respiration is possible. Among the lysosomal enzymes, acid phosphatases and beta-glucuronidase are found, the latter facilitating the turnover of the hyaluronic acid. There is no galactosidase, as the hyaluronic acid of the vitreous does not contain galactose.
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PMID:Histoenzymologic study of hyalocytes in tissue culture. 9 Apr 62

A new form of cytoplasmic glucose-6-phosphate dehydrogenase (E.C.1.1.1.49) was purified from rat liver by protamine sulfate precipitation, ammonium sulfate fractionation, ion exchange chromatography with diethylaminoethyl cellulose, and affinity chromatography with Cibacron blue agarose and NADP agarose. This form of the enzyme has a specific activity of over 600 units/mg of protein and gives essentially a single band by polyacrylamide gel electrophoresis. The form of the enzyme isolated by this purification method is 3 times more active than the form purified from liver by previously reported procedures. The relative mass of this pure glucose-6-phosphate dehydrogenase enzyme was determined by disc gel electrophoresis to be 269,000. This high activity glucose-6-phosphate dehydrogenase enzyme, after inactivation by reaction with palmityl-CoA, was no longer precipitated by specific rabbit and goat antisera to this purified enzyme. Thus, the possibility still exists that starved fat-refed animals contain glucose-6-phosphate dehydrogenase (G6PD) enzyme protein in an inactivated form no longer detectable by either enzyme activity or immunoprecipitation.
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PMID:Purification of a new high activity form of glucose-6-phosphate dehydrogenase from rat liver and the effect of enzyme inactivation on its immunochemical reactivity. 9 Jun 77

The author reports a modification of the UV method UltraZyme Plus alpha-Amyl Harleco and the adaptation to the Eppendorf Enzymautomat 5010. alpha-amylase acts on an oligosaccharide mixture yielding maltose, which is hydrolysed by alpha-glucosidase. The liberated glucose is determined specifically by the hexokinase/glucose-6-phosphate dehydrogenase (NAD+-dependent) method+ by addition of pyruvate, lactate dehydrogenase and ATP. Thereafter the lactate dehydrogenase reaction is stopped by addition of oxamate and the alpha-amylase activity is measured.
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PMID:[Kinetic determination of alpha-amylase in serum and urine with an oligosaccharide as substrate--modification for a fully mechanized enzyme measuring device (author's transl)]. 9 28

The activity of enzymes regulating the processes providing functional activity of leukocytes was studied in the exudate leukocytes of healthy rabbits and animals with alloxan diabetes. Rabbits with diabetes displayed a reduction of hexokinase, phosphoglucomutase, glucose-6-phosphate dehydrogenase and adenylate kinase activity. The activity of UDPH-pyrophosphorylase, UDPH-glycogentranspherase, 6-phosphogluconate dehydrogenase and glutathion reductase showed no significant changes in the exudate leukocytes in diabetes. A reduction of hexokinase and glucose-6-phosphate dehydrogenase limiting glycolysis and the pentose-phosphate cycle, respectively, providing energy for leukocytes and important in protein metabolism of these cells, is of great significance in the reduction of functional activity of leukocytes in the inflammatory focus in diabetes.
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PMID:[Enzymatic profile of the exudate leukocytes in diabetes mellitus]. 9 55

The problems encountered with a coupled enzyme assay for ATP using glucose, hexokinase and glucose-6-phosphate dehydrogenase are discussed and a modification where fructose and glucosephosphate isomerase were substituted for glucose is described. This modified assay was used successfully to measure the ATP synthesized by reversal of the sarcoplasmic reticulum ATPase. ATP synthesized by adenylate kinase contaminating the sarcoplasmic reticulum was easily corrected for by a subtraction procedure.
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PMID:A spectrophotometric assay of ATP synthesized by sarcoplasmic reticulum. 9 39

Biochemical studies were performed on blood and lung tissue of squirrel monkeys (Saimiri sciureus) following acute exposure to 0.75 ppm ozone (O3) for 4 h/d for 4 consecutive days. One group of animals was sacrificed at the end of the last exposure day and another group was sacrificed 4 d later after the last exposure. Evidence was sought for oxidation-induced changes known to occur in rodents when high levels of O3 are inhaled. A significant increase in red blood cell membrane fragility was observed, as well as significant decreases in red blood cell glutathione and erythrocyte acetylcholinesterase; however, the red blood cell enzymes, lactic acid dehydrogenase (LDH), and glucose-6-phosphate dehydrogenase (G6PDH) were not changed significantly. Lung tissue analysis showed that lipid peroxidation was markedly increased and tissue vitamin E levels were significantly decreased. The tissue enzymes G6PDH, glutathione reductase, and LDH significantly increased in activity. No significant changes were seen in either superoxide dismutase or malic acid dehydrogenase. The results of this experiment indicate that O3, or reaction products resulting from O3-tissue interaction in the lung, pass the air-blood barrier and are capable of producing biochemical changes in blood as well as in lung tissue.
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PMID:Biochemical response of squirrel monkeys to ozone. 10 43

The genetic rescue of Pgdn lethal alleles, accomplished by combining them with mutations lacking glucose-6-phosphate dehydrogenase activity, has led to the hypothesis that Pgdn lethality may be due to the accumulation of 6-phosphogluconate. In this article we report the rescue of Pgdn/Y males by dietary supplements (fructose and linolenate) designed to minimize 6-phosphogluconate production.
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PMID:Dietary rescue of a lethal "null" activity allele of 6-phosphogluconate dehydrogenase in Drosophila melanogaster. 10 8

Studies on liver homogenates obtained from Wistar rats revealed that the ageing process produces the loss of glucose-6-phosphate dehydrogenase activity and higher values in the thermolabile fraction of this enzyme. The biotrophic treatment with Gerovital H3 has a strong influence upon glucose-6-phosphate dehydrogenase with tendency to diminish the thermolabile fractions.
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PMID:Age differences in the glucose-6-phosphate dehydrogenase activity of homogenates from the liver of rats. The effect of gerovital H3 on the glucose-6-phosphate dehydrogenase activity. 10 18

Human erythrocyte lysate proteins were resolved into over 250 discrete spots by two-dimensional electrophoresis using isoelectric focusing in the first dimension and electrophoresis in the presence of sodium dodecyl sulfate, (SDS) in the second. The overwhelming excess of hemoglobin has made such analyses difficult in the past. However, with the ISO-DALT two-dimensional electrophoresis system, large numbers of red cell proteins can be mapped in the presence of hemoglobin. When hemoglobin and several other major proteins are removed by adsorption to DEAE-cellulose, additional minor components are seen, giving a total of over 275. With the use of purified preparations, the map positions of five cell enzymes or their subunits were determined: pyruvate kinase, catalase, glucose-6-phosphate dehydrogenase, hypoxanthine phosphoribosyltransferase, and carbonic anhydrase. The mapping techniques described complement and extend those traditionally used to find human red cell protein variants.
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PMID:Red cell proteins. I. Two-dimensional mapping of human erythrocyte lysate proteins. 10 31

The effects of K2PtCl4, cis-Pt(NH3)2Cl2, and trans-Pt(NH3)2Cl2 on the activities of glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, dihydrofolate reductase, fructose-1,6-bisphosphate aldolase, catalase, tyrosinase, and peroxidase have been investigated. All of the enzymes which are thought to have essential sulfhydryl groups (glyceraldehyde-3-phosphate dehydrogenase, aldolase, and glucose-6-phosphate dehydrogenase) were significantly inhibited by K2PtCl4. The other four enzymes studied are not known to have essential sulfhydryl groups, and were not significantly affected by the Pt compounds under the conditions employed. Glyceraldehyde-3-phosphate dehydrogenase was the only enzyme inhibited by all three Pt compounds tested, with K2PtCl4 being the most effective and cis-Pt(NH3)2Cl2 the least effective inhibitor. Semilogarithmic plots of residual activity versus inhibition time indicated that the inhibition reactions were not simple first-order processes, except for the inhibition of glucose-6-phosphate dehydrogenase by K2PtCl4 which appeared to be first-order with respect to enzyme concentration.
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PMID:The effects of platinum complexes on seven enzymes. 11 85


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