Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.9 (glucose-6-phosphatase)
 3,081 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intraperitoneal administration of diazepame and phenazepame into rats /at a dose 50 mg/kg/ within 4 days did not induce liver microsomal enzymes. After administration of chlordiazepoxide at the same dose content of cytochrome P-450 was increased and the rate of dimethylaniline demethylation was elevated. Content of protein as well as NADPH-cytochrome-c-reductase and glucose-6-phosphatase activities were increased after intraperitoneal administration of all the preparations at a dose 100 mg/kg within 4 days. Experiments on the potentiation of hexenal effect demonstrated the decrease in the time of sleep in animals, treated with chlordiazepoxide at a dose 100 mg/kg of body weight.
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PMID:[Effect of 1,4-benzodiazepine tranquilizers on the activity of the hepatocyte hydroxylating complex and glucose-6-phosphatase in white rats]. 4 17

The objective of this investigation was to find out whether vitamin E deficiency, apart from influencing the lipid component of cellular membranes, also influences the protein component. For that purpose a number of membrane-bound enzymes in the liver of the Pekin duckling were histochemically, cytochemically, and biochemically examined. Furthermore, cells, cellular membranes, and protein particles in membranes were morphometrically investigated. Histochemically five membrane-bound enzymes appeared to be stimulated in vitamin E deficiency: 5'-nucleotidase, glucose-6-phosphatase, isocitrate dehydrogenase (NADP), tetrazolium reductase (NADH), and tetrazolium reductase (NADPH). 5'-Nucleotidase and glucose-6-phosphatase were also investigated cytochemically and biochemically. The cytochemical localization of these enzymes was identical in control and vitamin E-deficient ducklings. Biochemically, a stimulation of these two enzymes also could be demonstrated. The increase per milligram of DNA appeared to be largest whereas the increase per milligram of protein, per milligram of phospholipid, and per milligram of RNA was only half of the increase per milligram of DNA. This can be explained by the 30 per cent increase of the cell volume in vitamin E deficiency leading to an increase of protein, phospholipid, and RNA per cell. The thickness of membranes and the diameter of protein particles in membranes were measured in liver parenchymal cells. In vitamin E deficiency the thickness of the outer mitochondrial membrane and the diameter of protein particles in this membrane were smaller whereas the thickness of the endoplasmic reticular membrane was larger. The increase of the activities of mitochondrial and microsomal enzymes and the decrease of the thickness of the outer mitochondrial membrane and of its protein particles are interpreted to be the result of the influence of free radicals on membranes with electron transport functions. The increase of 5'-nucleotidase activity in the plasma membrane is likely to have a different cause; it may be related to the transport of nucleotides across this membrane.
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PMID:Cellular membranes and membrane-bound enzymes in vitamin E deficiency. A histochemical, cytochemical, biochemical, and morphologic study of the liver of the Pekin duckling. 16 37

Female rats were injected subcutaneously with ethionine, and enzymic activities of liver membranes (Na+-k+-stimulated ATPase, Mg2+-stimulated ATPase, glucose-6-phosphatase, NADPH: cytochrome c oxido-reductase and NAD-nucleosidase) examined at proper intervals, during the intraperitoneal treatment of an egg phospholipid preparation (EPL). It is shown that EPL is unable to overcome the enzymic changes due to severe ethionine treatment, but is able to facilitate the recovery times after drug withdrawal for all the enzymic activities, except for NAD-nucleosidase. At lower dosage of the drug, the ethionine treatment is able to prevent the observed change of the glucose-6-phosphatase activity but not that of the Mg2+-ATPase. It is suggested that the EPL treatment may modify the chemical composition ahd/or architecture of liver membranes, altered by the ethionine injection, thus acting, at least partially, on the enzymic changes.
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PMID:The effect of egg phospholipid administration upon liver enzymic activities during ethionine treatment. 18 Dec 70

It is shown that human embryonic cells transformed by Rous sarcoma virus (stable cell line 23) and those transformed by polyoma virus (stable cell line P-2) are morphologically distinguished from the normal human embryonic cells. The mitotic activity of P-2 cells was 51% and the mitotic activity of 23 cells was 48%. While the mitosis activity of human embryo fibroblast was 28%. The duration of the mitosis of P-2 cells was 20 hours and that of 23 cells was 18 hr. The duration of the mitotic cycle of human embryo fibroblast was 18 hr. The G1 periods lasted 6 hours for both the cell lines; the S period of P-2 cells lasted 8 hr and the S period of 23 cells was 6 hr. Both the cell lines had a high content of RNA, DNA, protein bound SH-groups, and a high activity of acid phosphatase, acid RNAase and glucose-6-phosphatase. The content of glycogen, and acidic mucopolysaccharides, the activity of NADPH-tetrazolium reductase, succinic dehydrogenase of both the lines were the same as in normal human cells.
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PMID:Morphological and histochemical properties of human embryonic cells transformed by Rous and polyoma viruses. 19 87

In the experiment on rats the ethanol extract of propolis (EEP) injections caused an activation of all experimental enzymes. The greatest effect EEP exerted was on NADPH2 tetrazolium reductase and glucose-6-phosphatase.
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PMID:Biological properties and clinical application of propolis. V. The action of ethanol extract of propolis (EEP) on laboratory animals. Histochemical investigations. 20 Feb 48

The experiment was carried out on rats, which were divided into three experimental and one control groups. The experimental animals were intraperitoneally injected with furfural in the dose of 58 mg/kg body weight for 30 days. In the liver samples obtained at autopsy, apart from routine staining with hematoxylin and eosin, estimation of the activity of the following enzymes was made: succinic dehydrogenase. NADH-tetrazol reductase, lactic dehydrogenase, glucose-6-phosphate, adenosine-triphosphatase, Ca-formol, glucose-6-phosphatase and acid phosphatase. Glycogen content was also evaluated. A temporary decrease in the activity of reactions for the enzymes of tissue respiration, an increase in the activity of glucose-6-phosphatase with a simultaneous decrease of glycogen content, activation of intracellular digestive processes, and inhibition of active transport through biological membranes were found in animals intoxicated with furfural.
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PMID:[Morphological and histochemical changes in the rat liver in chronic furfural poisoning]. 20 22

Although the preparation of rat liver Golgi apparatus isolated by our method contains appreciable activities of NADH- and NADPH-cytochrome c reductases and glucose-6-phosphatase, these enzymes as well as thiamine pyrophosphatase of the extensively fragmented Golgi fraction are partitioned in aqueous polymer two-phase systems quite differently from those associated with microsomes. Similarly, the partition patterns of acid phosphatase and 5'-nucleotidase of the Golgi fragments differ from those of homogenized lysosomes and plasma membrane, respectively. It is concluded that most, if not all, of these marker enzymes in the Golgi fraction cannot be ascribed to contamination by the non-Golgi organelles. In sucrose density gradient centrifugation the NADH- and NADPH-cytochrome c reductase activities of the Golgi fraction behave identically with galactosyltransferase but differently from the reductase activities of microsomes, again indicating that the reductases are inherently associated with the Golgi apparatus. NADPH-cytochrome c reductase of the Golgi preparation is immunologically identical with that of microsomes. The marker enzymes mentioned above and galactosyltransferase behave differently from one another when the Golgi fragments are subjected to partitioning in aqueous polymer two-phase systems, suggesting that these enzymes are not uniformly distributed in the Golgi apparatus structure.
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PMID:Biochemical studies on rat liver Golgi apparatus. II. Further characterization of isolated Golgi fraction. 20 81

NADPH cytochrome c (cyt c) reductase and glucose-6-phosphatase, two enzymes thought to be restricted to the endoplasmic reticulum (ER) and widely used as ER markers, are present in isolated Golgi fractions assayed immediately after their isolation. Both enzymes are rapidly inactivated in fractions stored at 0 degrees C in 0.25 M sucrose, conditions which do not affect the activity of other enzymes in the same preparation. The inactivation process was shown to be dependent on time and protein concentration and could be prevented by EDTA and catalase. Morphological evidence shows that extensive membrane damage occurs parallel with the inactivation. Taken together with the immunological data in the companion paper, the findings indicate that the enzymes NADPH cyt c reductase and probably glucose-6-phosphate are indigenous components of Golgi membranes.
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PMID:Endoplasmic reticulum marker enzymes in Golgi fractions--what does this mean? 21 50

Light Golgi fractions (GF(1+2)) prepared from rat liver homogenates by a modification of the Ehrenreich et al. procedure (J. Cell Biol. 59:45) had significant NADPH-cytochrome P(450) reductase (NADPH-cyt c reductase) activity if assayed immediately after their isolation. An antibody raised in rabbits against purified microsomal and Golgi fractions. To find out whether this activity is located in bona fide Golgi elements or in contaminating microsomal vesicles, we used the following 3-step immunoadsorption procedure: (a) antirabbit IgG (raised in goats) was conjugated to small (2-5 mum) polycrylamide (PA) beads; (b) rabbit anti NADPH-cyt c reductase was immunoadsorbed to the antibody-coated beads; and (c) GF(1+2) was reacted with the beads carrying the two successive layers of antibodies. The beads were then recovered by centrifugation, and were washed, fixed, embedded in agarose, and processed for transmission electromicroscopy. Antireductase- coated beads absorbed 60 percent of the NADPH-cyt c reductase (and comparable fractions of NADH-cyt c reductase and glucose-6-phosphatase) but only 20 percent of the galactosyltransferase activity of the input GF(1+2). Differential vesicle counts showed that approximately 72 percent of the immunoadsorbed vesicles were morphologically recognizable Golgi elements (vesicles with very low density lipoprotein [VLDL] clusters or Golgi cisternae); vesicles with single VLDL and smooth surfaced microsome-like vesicles were too few (approximately 25 percent) to account for the activity. It is concluded that NADPH-cytochrome P(450) reductase is a Golgi membrane enzyme of probably uneven distribution among the elements of the Golgi complex.
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PMID:Presence of NADPH-cytochrome P-450 reductase in rat liver Golgi membranes. Evidence obtained by immunoadsorption method. 21 51

The effects of vitamin E deficiency on membrane integrity were studied by examining the temperature dependence of membrane-bound enzyme activities in liver mitochondria and microsome and in muscle sarcoplasmic reticulum. In vitamin E-deficient rabbits, the specific activities at 37 degrees of mitochondrial oligomycin-sensitive ATPase (EC 3.6.1.3), beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30), and microsomal glucose-6-phosphatase (EC 3.1.3.9) were increased, whereas those of microsomal NADH cytochrome C reductase (EC 1.6.99.3) and sarcoplasmic reticulum Ca-ATPase were reduced in comparison to control rabbits. Arrhenius plots of activity against temperature yielded a linear plot over the range 10 to 40 degrees in the case of beta-hydroxybutyrate dehydrogenase, NADH cytochrome C reductase and Ca-ATPase, and multiple discontinuities for glucose-6-phosphatase and oligomycin-sensitive ATPase. In control rabbits, all five enzymes showed a single discontinuity in the Arrhenius plot over the range 16 to 19 degrees. These results reflect changes in the microenvironment of membrane-bound enzymes as a consequence of vitamin E depletion.
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PMID:Effects of vitamin E deficiency on the activities of lipid-requiring enzymes in rabbit liver and muscle. 22 Mar 97


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