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PubMed1978

[Influence of temperature and salinity on glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in mussel (Mytilus edulis, L.) (author's transl)].

The activity of Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in mussel hepatopancreas and gill tissues decreases with the salinity of sea water. A decrease in both activities is observed during the first few days in the hepatopancreas of mussel starved at temperatures upper and below the natural thermal habitat; later, the levels of enzymes experience a transitory rise. The influence of temperature on the Km of 6-phosphogluconate dehydrogenase for the hepatopancreas was studied. Minimum value correspond to the nearest temperature to that of the mussel natural habitat.

Animals↗
PubMed1969

The foetal development of lactate dehydrogenase isoenzymes, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from human striated muscle.

1. Human foetal skeletal muscles involved in support and in periodic contractility were studied for their content of total extractable lactate dehydrogenase, glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities as well as for the relative distribution of lactate dehydrogenase isoenzymes. 2. During foetal development a linear steady increase in total lactate dehydrogenase activity as well as a linear decrease in the H/M sub-unit ratio of the isoenzymes was found. 3. No significant changes were found in the activities of the enzymes of the hexose monophosphate shunt (C-6 oxidation). 4. The changes found suggest a steady increased synthesis of lactate dehydrogenase M-sub-units in human skeletal muscles during foetal development. 5. The weekly changes in the total lactate dehydrogenase activity and in lactate dehydrogenase isoenzymes are lower in muscles involved in support than in those involved in periodic contractility. 6. These findings, together with the literature available, are consistent with the morphological fact that foetal development of skeletal muscles mostly concerns the white muscle fibres and not the red muscle fibres.

Female↗
PubMed1983

Age-related changes in glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in the subcellular fractions from the rat brain and the effect of dimethylaminoethanol.

The activity of pentose phosphate pathway enzymes (glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase) was measured in the cytosol and the particulate fractions (mitochondrial-synaptosomal and microsomal) from the cerebrum and the cerebellum of the rats aged 1, 2, 3, 6, 9 and 12 months. The results showed that the two enzymes occurred both in cytosol and particulate fractions. Both the enzymes were higher in the particulate fractions from cerebellum than in the same fractions from cerebrum. In both regions of the brain, particulate fraction enzymes showed an age-related decline in their activity, but the cytosol fraction enzymes remained unchanged in all the age groups. Dimethylaminoethanol, an important molecular constituent of some antiageing drugs, increased the activity of these enzymes in a dose dependent manner only in the particulate fractions.

Aging↗
PubMed1984

The inhibitory effect of actinomycin D and cycloheximide on the increase in activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in experimentally induced diseased skeletal muscles.

The myotoxic effect of the subcutaneous administration of N,N1-dimethyl-p-phenylenediamine (DPPD) in rats was enhanced by the simultaneous administration of hyaluronidase. The resulting myopathy was associated with an early and dramatic increase in activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase. Administration of actinomycin D or cycloheximide prior to the combined DPPD and hyaluronidase treatment prevented the increase in activity of both pentose phosphate pathway enzymes, indicating that the increase in activity requires RNA synthesis and protein synthesis. The possibility that the increase in activity of both NADPH-regenerating enzymes results from the modification by effectors of existing less active forms of these enzymes leading to more highly active forms was refuted.

Animals↗
PubMed1986

Selective precipitation of phosphofructokinase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from rat erythrocyte hemolysates by polyethylene glycol.

Precipitation profiles of phosphofructokinase, glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase have been established in the range of 0-16% PEG at different pH values. Precipitation generally occurred between narrow limits of polyethylene glycol. The polymer concentration needed to reach any level of enzyme precipitation is dependent on pH. Particular conditions (% PEG and pH) for the selective enzyme enrichment have been determined.

Animals↗
PubMed1981

The increase in activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in skeletal muscles of rats after subcutaneous administration of N,N'-dimethyl-para-phenylenediamine.

After subcutaneous administration of N,N'-dimethyl-para-phenylenediamine (DPPD) in rats, a myogenic myopathy was produced in the skeletal muscles. In this communication, the results of the application of various histochemical techniques for the localization of oxidoreductases, transferases, hydrolases and isomerases and biochemical techniques for the estimation of activities of oxidoreductases in the experimental skeletal muscles are presented. The most striking results was the activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase which increased dramatically during the early phase of the muscle disease. The increase in activity of the pentose phosphate shunt enzymes was the first pathological alteration and was present as early as 8 h after a single injection of DPPD. Histochemical techniques for demonstration of activity of both enzymes are therefore highly suited for the detection of minor diseases and the early onset of major diseases of the neuromuscular system. Some glycolytic enzymes as well as some enzymes of the aerobic part of the metabolism showed an early decrease or increase in activity indicating a metabolic imbalance in the muscle fibres. There were more fibres with an intermediate pattern of the energy yielding enzymes in the experimental muscle specimens then in specimens from the control groups. The activity of the catabolic hydrolytic enzymes was strongly increased in pathological muscles. The aerobic muscles were more vulnerable to DPPD than the anaerobic muscles.

Animals↗
PubMed2000

Lobular distribution pattern of lactate dehydrogenase and 6-phosphogluconate dehydrogenase activity in rat liver.

Lactate dehydrogenase (LDH) and 6-phosphogluconate dehydrogenase (6-PGDH) activities were measured in lobular areas expanding between 3 portal tracts and an efferent central vein in the livers of male Wistar rats, using a Lowry technique. The maximum of LDH activity was found in a nearly uniform broad area in the lobular periphery. From that area values decreased along periportal/septal-->perivenous gradients, but only slightly within that area along the periportal-->septal axis of the vascular septum. Maximum values of 6-PGDH activity were present in an intermediate area close to the central vein demonstrating a rather inhomogeneous distribution pattern without a clear definition of zonal limits. Our data on the distribution pattern of LDH are in agreement with the concept of the metabolic lobulus and are supported by a recent evaluation of the vascular architecture in rat liver. The lobular distribution pattern of 6-PGDH cannot be interpreted without doubt in accordance with that concept.

Animals↗
PubMed1975

Regulation of glucose-6 phosphate dehydrogenase and 6-phosphogluconate dehydrogenase in the meal-fed rat.

Meal-feeding of a high sucrose diet produces a diurnal cycle (i.e., food response) in glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) levels resulting in an elevated level of these enzymes at approximately 12 hours after the start of a 2-hour meal and a return to base level by 24 hours. The effects of actinomycin D and cycloheximide on the 12-hour increases in G6PD and 6GPD were determined. Cycloheximide completely blocked the increase in G6PD if administered 2 or 4 hours after start of the meal, while actinomycin D completely blocked the increase in G6PD if administered at 2 hours and almost completely at 4 hours after start of the meal. These results were obtained previously with starved rats refed a sucrose diet. The diurnal increases in G6PD and 6PGD in meal-fed rats and the induction of G6PD in starved-refed rats thus appear to be regulated by the same mechanism requires RNA synthesis within 4 hours after start of re-feeding. The response of 6PGD to cycloheximide and to actinomycin D at 2 or 4 hours after start of the meal is essentially the same as that of G6PD. These data suggest that the increases in G6PD and 6PGD (and other enzymes) brought about by carbohydrate refeeding AFTER starvation or by carbohydrate meal-feeding on a diurnal cycle are mediated by a rapid change in RNA synthesis. This appears most compatible with a coordinate control of gene expression through messenger RNA synthesis.

Animal Nutritional Physiological Phenomena↗
PubMed1989

Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Lactobacillus casei: responses with different modulators.

Glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were separated and partially purified from glucose-grown cells of Lactobacillus casei. The enzymes had similar pH optima, thermosensitivity and molecular weights. They had different net charges and their pI values were 5.38 and 4.52, respectively. Histidine, arginine, lysine and cysteine residues were essential for the activity of G6PD, and all the above amino acids with the exception of lysine were required for 6PGD activity. Mg2+ activated 6PGD up to 15 mM concentration, above which it was inhibitory. It had no effect on G6PD activity. G6PD was specific for NADP+, but 6PGD showed some activity with NAD+ as the cofactor, although it was essentially NADP(+)-preferring. Both the enzymes, were inhibited by NADPH. 6PGD was also inhibited by its product, ribulose 5-phosphate. ATP inhibited 6PGD only at subsaturating concentrations of NADP+. The inhibition was sigmoidal in the absence of Mg2+ and hyperbolic in its presence.

Glucosephosphate Dehydrogenase↗
PubMed1982

Coordinate regulation of the pentose phosphate pathway and of the activity of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase (decarboxylating).

The activities of glucose-6-phosphate dehydrogenase (GPD) and 6-phosphogluconate dehydrogenase (decarboxylating) (PGD) in Saccharomyces cerevisiae were found to change by a factor similar to the reported changes in the rate of the pentose phosphate pathway between cells grown in minimal medium and in rich medium. It is suggested that the rate of this pathway is regulated not only by the activity of GPD, a well-known key enzyme, but also by PGD. These two enzymes seem to function in a coordinated fashion.

Amino Acids↗
PubMed1980

Prolactin, thyrotrophin interaction in the regulation of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities in rat mammary glands.

The roles of prolactin and thyrotrophin (TSH) in the regulation of glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) activities in rat mammary glands were investigated by the administration of thyroid hormone-releasing hormone (TRH), bromocriptine, prolactin, TSH and triiodo-1-thyronine (T(3)). TRH failed to induce changes in the activities of these enzymes in glands from intact animals but the releasing hormone significantly increased the activities of both the enzymes in the glands of ovariectomized and adrenalectomized animals. Bromocriptine administration had no effect on the activities in both, intact and ovariectomized-adrenalectomized animals. Administration of ovine prolactin to hypophysectomized rats did not affect the activities of these enzymes. On the other hand treatment with TSH resulted in significant increases in the activities. On the other hand treatment with TSH resulted in significant increases in the activities. Similarly, administration of T(3) to these animals resulted in changes similar to those observed after TSH administration. Combined administration of prolactin and TSH showed that prolactin is capable of partially inhibiting the TSH-induced increases. It is concluded that TSH is involved in the channelling of substrates into the pathways of nucleic acid synthesis and prolactin probably plays a regulatory role in this process.

Animals↗
PubMed1982

Separate detection of glucose-6-phosphate dehydrogenase from 6-phosphogluconate dehydrogenase by DEAE-paper chromatography.

Red blood cell lysates were applied to DEAE cellulose paper for detection of glucose-6-phosphate dehydrogenase. Glucose-6-phosphate dehydrogenase (G-6-PD) was separated from 6-phosphogluconate dehydrogenase (6-PGD) by DEAE-cellulose paper-chromatography and their activities were detected on the chromatogram by applying the reaction mixture. The fluorescence of NADPH formed by G-6-PD was not interfered with by 6-PGD activity. This is a sensitive procedure which detects slight loss of G-6-PD in red blood cells and could be applied to the detection of G-6-PD deficiency.

Chromatography, DEAE-Cellulose↗
PubMed1990

Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities in normal canine mammary gland and in mammary tumours and their correlation with oestrogen receptors.

Glucose-6-phosphate dehydrogenase (G-6-PD) and 6-phosphogluconate dehydrogenase (6-PGD) activities were studied in 10 normal canine mammary glands and in 19 canine mammary tumours, which included seven benign and 12 malignant neoplasms. The malignant tumours were also examined for oestradiol receptors. The mean G-6-PD and 6-PGD activities were 5.17 +/- 1.84 and 1.65 +/- 0.64 IU per g protein in normal glands, 8.8 +/- 2.7 and 3.8 +/- 0.99 IU per g protein in benign and 19.6 +/- 5.2 and 8.5 +/- 2.1 IU per g protein in malignant mammary tumours. The enzyme activities were significantly higher in tumour tissue than in normal glands. Malignant tumours had much greater activity than benign. With the increasing anaplasia, there was a corresponding rise in the activity of the two enzymes. There was an inverse correlation between the oestrogen receptor (ER) status and the enzyme activity. The ER-positive tumours had low and ER-negative tumours had high enzyme activities.

Animals↗
PubMed1980

Control by phospho-adenosinediphospho-ribose of NADP-dependent isocitrate dehydrogenase and 6-phosphogluconate dehydrogenase in Streptomyces griseus.

The metabolic function of NAD(P)-glycohydrolase in the streptomycin-producing Streptomyces griseus was investigated. Phospho-adenosinediphospho-ribose, the product of NAD(P)-glycohydrolase reaction was shown to interfere as a competitive inhibitor not only with the glucose-6-phosphate dehydrogenase (VORONINA et al. 1978) but also with the NADP-dependent isocitrate and 6-phospho-gluconate dehydrogenases. Inhibition kinetics were studied with isocitrate dehydrogenase from pig heart and 6-phosphogluconate dehydrogenase from yeast as well as with mycelial extracts of a mutant of S. griseus lacking NAD(P)-glycohydrolase.

Adenosine Diphosphate Ribose↗
PubMed1979

Purification and properties of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from a methanol-utilizing yeast, Candida boidinii.

Glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate: NADP oxidoreductase, EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (6-phospho-D-gluconate: NADP oxidoreductase, EC 1.1.1.44) were purified approx. 1700 fold and 330 fold, respectively, from Candida boidinii grown on methanol. The final enzyme preparations were homogeneous as judged by polyacrylamide gel electrophoresis. The molecular weights of the enzymes were estimated to be 118 000 and 110 000, respectively. Both enzymes are composed of two probably identical subunits and the molecular weights of the polypeptide chains were calculated to be 61 000 and 58 000, respectively. From a consideration of enzyme activities and types of inhibition by different metabolites the role of these two enzymes in glucose- and methanol-metabolism is discussed.

Candida↗
PubMed1977

Schistosoma mansoni and Schistosoma japonicum: comparison of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase activities in adults.

Glucose-6-phosphate dehydrogenase activity in paired adult Schistosoma mansoni is about twice as great as in paired adult Schistosoma japonicum. 2. 6-phosphogluconate dehydrogenase activity accounts for 25.8% of the measured production of reduced nicotinamide adenine dinucleotide phosphate (NADPH) in S. japonicum but only 8.6% of the measured production of NADPH in S. mansoni. 3. These data suggest a species difference in 6-phosphogluconate metabolism.

Animals↗