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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)

1. The activities of the oxidative enzymes (glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase) and of the non-oxidative enzymes (transaldolase, tranketolase, ribose 5 phosphate isomerase and ribulose 5-phosphate 3-epimerase) of the pentose phosphate pathway were measured at various times during the first 24h of skeletal-muscle regeneration after administration of Marcaine, a mytoxic local anesthetic. 2. The activities of the oxidative enzymes increased after Marcaine injection and rose to 9 times control activities by 24h. 3. The activities of all non-oxidative enzymes were increased after Marcaine administration, but to a much smaller extent than the oxidative enzymes (1.1-1.7-fold). 4. Histochemical analysis localized glucose 6-phosphate dehydrogenase activity within muscle fibres of control and Marcaine-treated muscles. 5. Cycloheximide or actinomycin D prevented the increase in oxidative enzyme activities, suggesting a requirement for synthesis of protein and RNA.
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PMID:The pentose phosphate pathway in regenerating skeletal muscle. 62 75

The activities of three enzymes of the hexose monophosphate pathway (HMP) were measured in frozen samples of rat cerebral cortex and ethylnitrosourea-induced tumors of the rat nervous system. Results show that in most tumors, adequate amounts of glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), and transketolase (TK) were present so as not to be rate-limiting for utilization of the HMP. When enzyme activites were expressed on the basis of fresh weight, TK was increased in most tumors as compared with cerebral cortex; G6PDH and 6PGDH were more variable, showing either higher or lower activities in tumors as compared to control. Tumors in general had a lower protein content than cerebral cortex. When activities were expressed in terms of this protein content, mean values for the dehydrogenases in all groups of tumors were higher than the average value in cortex, indicating that G6PDH and 6PGDH were spared in tumors relative to other proteins. TK activities in tumors, expressed in terms of cytosol protein were lower than or in the same range as cortex. Increased activities of HMP enzymes in some tumors indicated that the potential activity of the HMP in some (but not all) tumors of the nervous system is greater than that of cerebral cortex.
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PMID:Activities of enzymes of the hexose monophosphate pathway in nervous system tumors induced by ethylnitrosourea. 64 60

Cultured skin fibroblasts from subjects with progeria contain an increased fraction of heat-labile enzymes and other altered proteins. To determine whether freshly obtained cells are similarly affected, erythrocytes from a progeric female and her clinically normal parents were analyzed for heat-lability of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Hemolysates of the child's whole erythrocyte populations and young erythrocytes isolated by equilibrium density centrifugation contained significantly higher heat-labile fractions of both enzymes compared to control hemolysates. Values in both parents were intermediate to those of their daughter and controls, consistent with autosomal recessive inheritance in this family. The primary source of these multiple protein defects is unknown but may reside in a mutant gene producing abnormal protein turnover or defective DNA repair. An increased fraction of thermolabile enzymes in circulating erythrocytes should be useful in identifying persons at risk for progeria and other disorders of premature aging.
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PMID:Heat-labile enzymes in circulating erythrocytes of a progeria family. 65 63

Erythrocyte glucose-6-phosphate dehydrogenase activity is measured with a centrifugal analyzer by use of a commercial reagent kit and of the reaction glucose-6-phosphate + NADP+ leads to 6-phosphogluconolactone + NADPH. Rate of production of NADPH is measured and related to hemoglobin concentration. Maleimide is added to inhibit further production of NADPH in a secondary reaction by endogenous 6-phosphogluconate dehydrogenase. The method is compared with others that are designed to circumvent the secondary reaction by either (a) addition of excess phosphogluconate dehydrogenase to drive the secondary reaction to completion or (b) inhibition of endogenous phosphogluconate dehydrogenase by 2,3-diphosphoglycerate. The present method has the advantages that reaction rate more quickly becomes linear and reagent cost is less as compared with other methods. The within-run coefficient of variation was 3%. The various methods investigated showed good statistical correlation.
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PMID:Maleimide as an inhibitor in measurement of erythrocyte glucose-6-phosphate dehydrogenase activity. 65 77

Activity of dehydrogenases related to pentosephosphate pathway was not distinctly altered in soluble fraction of kidney cortex and medulla after 48 and 72 hrs of starvation. In diabetes the activity of these enzymes in rat kidney, as distinct from liver tissue, was not decreased but it was elevated and within 72 hrs after administration of alloxan the activity of glucose-6-phosphate dehydrogenase was increased 2-fold and the activity of 6-phosphogluconate dehydrogenase was increased by 30% above the normal level. Content of free fatty acids was also increased in kidney cortex of diabetic rats within 72 hrs after administration of alloxan. Alterations in content of free fatty acids were not observed either in kidney of diabetic animals within other studied periods (6 and 14-16 days) of treatment or in the tissue of starved rats. The data obtained suggest that free fatty acids do not participate immediately in controlling effect on dehydrogenases of pentosephosphate pathway in kidney in vivo.
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PMID:[Effect of starvation and diabetes on the activity of glucose-6-phosphate and 6-phosphogluconate dehydrogenases and on the free fatty acid content of rat kidney cortex and medulla]. 66 69

In this communication the results of applying various histochemical semipermeable membrane techniques to the localization of several enzymes in bovine and porcine heart are presented. The Purkinje fibers of the atrioventricular conducting system of the bovine heart differ from the myocardium proper in containing a greater activity of the glycolytic and gluconeogenetic enzymes--lactate dehydrogenase, glyceraldehyde-phosphate dehydrogenase, hexokinase, glucosephosphate isomerase and phosphoglucomutase, and less activity of the aerobic enzymes--NADH: nitroBT oxidoreductase and isocitrate dehydrogenase (NADP+). The metabolic reactions obtained with Purkinje fibers of the porcine heart are less pronounced. These histochemical findings are in accordance with the impression that Purkinje fibers, compared with the common myocardial fibers, have a higher rate of anaerobic metabolism and a lower rate of aerobic metabolism. The activity of the NADPH regenerating enzymes glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase (decarboxylating), and the activity of acid hydrolases such as non-specific esterase and acid phosphatase is higher in the Purkinje fibers of both the bovine and porcine heart.
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PMID:Enzyme histochemical studies on the Purkinje fibers of the atrioventricular system of the bovine and porcine hearts. 66 82

1. Measurements have been made of the activities of enzymes of the glycolytic route, the pentose phosphate pathway, the tricarboxylic acid cycle and lipogenesis in liver and adipose tissue from genetically obese (fa/fa) rats and their lean litter mates (fa/ --). The effect of food restriction for a period of three weeks on the enzyme profile of liver and adipose tissue of the obese rat was also studied. 2. The most striking increases in enzyme activity in livers from obese rats were: (a) among enzymes of lipogenesis; ATP-citrate lyase, acetyl-CoA carboxylase, fatty acid synthetase, malate dehydrogenase (decarboxylating) and cytoplasmic glycerolphosphate dehydrogenase; (b) within the pentose phosphate pathway; glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase; (c) within the glycolytic pathway; glucokinase, pyruvate kinase and lactate dehydrogenase. All of these enzymes showed a significant increase in activity on the basis of U/g liver and U/mg DNA. In adipose tissue all the enzymes of lipogenesis, of the glycolytic route, of the oxidative segment of the pentose phosphate pathway and of the tricarboxylic acid cycle were increased when expressed as U/2 fat pads or as U/mg DNA. 3. The restriction of the food intake of obese rats to that consumed by their lean litter mates for periods of three weeks did not produce the expected adaptive decrease in enzymes of lipogenesis; in adipose tissue, only ATP-citrate lyase and malate dehydrogenase (decarboxylating) showed a marked decrease; no significant change was found in adipose tissue or liver of the activities of acetyl-CoA carboxylase and fatty acid synthetase, when expressed on a cell basis (U/mg DNA). The non-oxidative enzymes of the pentose phosphate pathway and enzymes involved in glycerogenesis (pyruvate carboxylase, malate dehydrogenase and phosphoenolpyruvate carboxykinase) all increased in adipose tissue from limit-fed obese rats. 4. The rate of conversion of specifically labelled glucose to (14C)O2 and 14C-labelled lipid by pieces of adipose tissue and by liver slices was also measured. Insulin caused an increase in the conversion of (1-14C)glucose to (14C)O2 and 14C-labelled lipid in obese rats fed ad libitum, limit-fed rats and in their lean litter mates. 5. The results are discussed in relation to the raised insulin and hypothyroid state of the obese rat. The effect of this altered hormonal status on the activity of cyclic nucleotide phosphodiesterases and cellular levels of adenosine 3' :5'-monophosphate and guanosine 3' :5'-monophosphate and guanosine 3' :5'-monophosphate in relation to the obese syndrome is considered.
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PMID:Adaptive responses of enzymes of carbohydrate and lipid metabolism to dietary alteration in genetically obese Zucker rats (fa/fa). 71 Mar 95

The ratios of some key enzymatic activities of carbohydrate metabolism have been measured in human tumor cytosols. The activities of whole hexokinase (low Km, EC 2.7.1.1 and high Km, EC 2.7.1.2), 6-phosphogluconate dehydrogenase (EC 1.1.1.43), glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and glucose-6-phosphate isomerase (EC 5.3.1.9) change according to a biochemical pattern coherent with cell growth requirements. 6-phosphogluconate dehydrogenase activity was in each sample tested higher than glucose-6-phosphate dehydrogenase activity; this indicates that 6-phosphogluconate, a powerful inhibitor of glucose-6-phosphate isomerase, is unlikely to accumulate and inhibit this enzyme and glucose-6-phosphate channelling into glycolysis.
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PMID:6-phosphogluconate dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphate isomerase, and hexokinase activity ratios in some human tumor cytosols. 74 21

1. The haemoglobin content of developing erythroblasts was shown to increase rapidly when the cells completed the final cell division of erythroid development and passed from the dividing into the non-dividing cell compartment. 2. The activity of carbonic anhydrase was measured and shown to increase continually throughout erythroid differentiation. The activity increased most rapidly in the polychromatic stage. 3. Catalase activity did not increase significantly during erythroid differentiation until the reticulocyte stage. 4. The activity of four enzymes, glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, adenosine deaminase and nucleoside phosphorylase, exhibited a similar pattern of change during erythroid differentiation. In the dividing cell compartment their activity was relatively high but exhibited a steep decline between the polychromatic stage and the orthochromatic stage, that is, as the cell completed its final cell division and moved from the dividing to the non-dividing compartment. After this the activity of these enzymes was stabilized at a relatively low value, and this activity persisted at such a value until the reticulocyte stage. 5. Lactate dehydrogenase activity also declined after the cell had crossed from the dividing into the non-dividing stage, but in this case the decline was less than in the case of the above four enzymes. 6. Adenylate kinase activity was relatively constant in the dividing cell compartment but exhibited a 60 percent increase when the cell passed from the dividing into the non-dividing compartment. 7. The cessation of cell division appears to coincide with a set of complex biochemical changes.
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PMID:Biochemical and enzymic changes during erythrocyte differentiation. The significance of the final cell division. 80

Anthropological studies were done on 1276 Libyans from the Mediterranean cities of Tripoli and Benghazi, and from Sabha southward in The Sahara. The incidences of hemoglobin (Hb)-S and glucose-6-phosphate dehydrogenase (G-6-PD) deficiency were low in the coastal areas and significantly high in Sabha. Hb-C occurred sporadically in Tripoli and Sabha, and was absent from Benghazi in the east. One case of Hb-J Benghazi was noted. There were no sigificant differences in the ABO blood group and Rh0 (D) type distributions in the three localities. G-6-PD gene GdAfrequency was significantly high in Sabha. The lowest value of 6-phosphogluconate dehydrogenase (6-PGD) gene PGDA frequency and highest value of the gene PGDC were in Sabha. Adenylate kinase (AK) gene AK2 was only detectable in Tripoli. Acid phosphatase (AP) gene Pa frequency in Sabha was more than twice that in Tripoli and Benghazi, while pc was distinctly lower in Sabha than in the northern cities. Haptoglobin gene Hp1 frequency was almost identical in all areas. Anthropometric measurements revealed overall homogeneity of the three samples, closer similarity in the coastal region to adjacent North African populations, and Negroid influence in the Sahara Libyans. Anthropometry substantiated findings from blood markers.
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PMID:Anthropological studies among Libyans. Erythrocyte genetic factors, serum haptoglobin phenotypes and anthropometry. 80 38


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