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)

Localization and activities of alkaline phosphatase, ATPase, 5-nucleotidase, glucose-6-phosphatase, thiamine pyrophosphatase and nucleoside diphosphatase were studied in the miracidium of Fasciola hepatica L. Except for nucleoside diphosphatase whose activity in the miracidium was not observed, all the enzymes were most active in the archenteron, protonephridia and nerve ganglion. This localization of the reaction intensity allows the inference that the three organs mentioned are sites of both intense carbohydrate metabolism and lively active transport. The role of phosphatases in carbohydrate metabolism is discussed.
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PMID:Specific and non-specific phosphatases in the miracidium of Fasciola hepatica L. 17 37

The activities of 5-nucleotidase (Ec.3.1.3.5), alkaline phosphatase (Ec.3.1.3.1), glucose-6-phosphatase (Ec.3.1.3.9), and ribonuclease (Ec.3.1.13) had been measured in tissue homogenate and in haemolymph of Biomphalaria alexandrina, the specific intermediate host for the parasitic disease schistosomiasis, induced by the parasite Schistosoma mansoni.
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PMID:Activity of some hydrolytic enzymes in tissue homogenates and haemolymph of fresh water snails, intermediate hosts in schistosomiasis. 165 90

It was established that acrylonitrile (AN) toxic action resulted in changes in the morphofunctional characteristics of white blood cells. Deviations were found in the activity of the marker enzymes of alkaline phosphatase neutrophil secretory granules and myeloperoxidase. Other changes were established in the markers of acid phosphatase lysosomes, the enzyme of plasma membrane--5 nucleotidase, in the endoplasm network of glucose-6-phosphatase, in succinate dehydrogenase mitochondria, and in alpha-glycerolphosphate dehydrogenase. Along with a considerably lowered succinate dehydrogenase activity, lymphocyte cell deformation against the activity of this enzyme was detected. The data obtained specified newly revealed changes in the blood at AN intoxication and indicated to innovated means of its prophylaxis.
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PMID:[Study of the activity of membrane-bound leukocyte enzymes in chronic acrylonitrile poisoning in experimental studies and occupational environment]. 196 27

The amphiphilic cationic cardioactive drugs (pindolol, propranolol and amiodarone) were tested for their effects on lipid dynamics (measured by fluorescence depolarization) and on enzymatic activities up to 1 mM in purified cardiac sarcolemmal vesicles from adult rat. The vesicles were enriched 12- to 37-fold (with respect to tissue homogenate) in Na+/K+ ATPase, K+-stimulated p-nitrophenylphosphatase, 5'nucleotidase and adenylate cyclase, all of which are believed to be components of sarcolemma. Phospholipids and cholesterol content were enriched 5- and 13-fold respectively. There was very little contamination of the sarcolemmal vesicles by sarcoplasmic reticulum (as judged by Ca2+ ATPase and glucose-6-phosphatase activities) or mitochondria (as judged by cytochrome-c-oxidase activity). Pindolol had no effect on lipid dynamics and enzyme activities except for the isoproterenol-stimulated adenylate cyclase. The latter was also totally inhibited at 1 microM by propranolol which inhibited Mg2+ ATPase and increased fluidity above 20 microM. Amiodarone affected all the enzyme activities (except Na+/K+ ATPase): isoproterenol-stimulated adenylate (IC50 = 30 microM), Mg2+ ATPase (IC50 = 20 microM) and K+-stimulated-p-nitrophenylphosphatase were inhibited; 5'nucleotidase was activated above 2 microM. By contrast with propranolol, amiodarone decreased lipid mobility. The effect was linear with the concentration of the drug above 1 microM.
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PMID:Differential effects of amiodarone and propranolol on lipid dynamics and enzymatic activities in cardiac sarcolemmal membranes. 253 21

Histochemical methods were used to study the localization and activity of acid and alkaline phosphatases, ATP-ase, 5-nucleotidase, and glucose-6-phosphatase in tissues of the mature form of Hymenolepis nana. Considerable differences in activity and localization of particular enzymes were observed in the organs of the parasite. The results obtained permit the statement that the integument is the most active enzymatically; in connection with the literature data, this gives grounds for the thesis that the integument of the cestodes functions as an absorbent-digestive organ.
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PMID:The activity of some phosphatases in tissues of adult Hymenolepis nana Siebold (Csetoda). 255 20

An alkaline 5'-nucleotidase with properties similar to those of membrane-bound 5'-nucleotidase was recovered in soluble form in the postmicrosomal supernatant fraction (cytosol) of rat liver. The enzyme seems to constitute a quantitatively distinct fraction, since the activity in postmicrosomal supernatants was increased by a further 10% by additional homogenization of livers. Lysosomal acid phosphatase activity increased similarly, whereas other membrane-bound marker enzymes alkaline phosphatase, phosphodiesterase I and glucose-6-phosphatase showed no increase when homogenization of liver tissue was continued. Gel-permeation chromatography and pH-dependence studies indicated that enzyme activity in the supernatant fraction with 0.3 mM-UMP or -AMP as substrate at pH 8.1 was about 85 or 100% specific respectively. In regenerating liver the enzyme recovered in soluble form showed decreased specific activity, in contrast with alkaline phosphatase measured for comparison. The nucleotidase activity per mg of cytosolic protein was 2.1 nmol/min with AMP as substrate. The total activity measured in the postmicrosomal supernatant was 1.5% of the homogenate activity measured in the presence of detergent.
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PMID:The presence and activity in normal and regenerating rat liver postmicrosomal supernatant fraction of an enzyme with properties similar to those of membrane-bound 5'-nucleotidase. 302 68

The studies on the effects of phenol (P), 2,4-dinitrophenol (DNP), pentachlorophenol (PCP) individually and in three combinations, viz., (PCP + DNP)/P (highly antagonistic), (DNP + P)/PCP (additive), and (P + DNP)/PCP (highly synergistic), at three sublethal levels (1/10, 1/15, and 1/20 of the 96-hr LC50) on the activity of hydrolytic enzymes (acid, alkaline, and glucose-6-phosphatases and 5-nucleotidase) in the brain and kidney of a fresh-water teleost, Notopterus notopterus revealed inhibition of enzyme activity after 15 and 30 days of exposure. Maximum inhibition (-89.32%) was observed in acid phosphatase activity in brain at 1/10 concentration of (P + DNP)/PCP combination after 30 days, but minimum (-3.64%) in activity of glucose-6-phosphatase in kidney at 1/20 of (PCP + DNP)/P combination after 15 days of exposure. However, biphasic effects of P, DNP, and (PCP + DNP)/P combination were observed in kidney, i.e., inhibition of enzymes activity at higher concentrations and stimulation at lower concentrations after both time intervals.
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PMID:Physiological stress induced by sublethal concentrations of phenolic compounds in Notopterus notopterus: measurement of hydrolytic enzymes. 303

The activity of sodium-potassium-activated adenosine triphosphatase (Na-K-ATPase) is considerably higher in homogenates of outer medulla than in the cortex or papilla of the kidney. The enzyme has similar kinetic characteristics in both cortex and medulla, and binds ouabain in the same proportion. The discrepancy in enzymatic activity is not paralleled by similar change in the activity of adenyl cyclase, 5'nucleotidase, glucose-6-phosphatase, or succinic dehydrogenase. Na-K-ATPase is also higher in distal convoluted tubules (ventral slices) than in the proximal tubules (dorsal slices) of the kidney of Amphiuma. The high concentration of Na-K-ATPase in the red medulla of the kidney is probably related to the presence here of the thick ascending limb of the loop of Henle, and this has important implications with regard to the mechanism of sodium reabsorption by different portions of the nephron.
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PMID:The distribution of sodium-potassium--activated adenosine triphosphatase in medulla and cortex of the kidney. 432 13

Non-specific and specific phosphatases have been histochemically localized in the tissues of Avitellina lahorea, an intestinal parasite of sheep and goats. Large quantities of acid phosphatase, alkaline phosphatase and adenosine triphosphatase were observed in almost all organs except the parenchyma where there were moderate amounts of acid phosphatase and no alkaline phosphatase; the reproductive ducts contained moderate amounts of alkaline phosphatase. 5-nucleotidase was observed only in the uterus, egg pouches and eggs and glucose-6-phosphatase activity was restricted to the tegument. The probable functions of these moieties at different sites are discussed.
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PMID:Histochemical localization of phosphomonoesterases in Avitellina lahorea Woodland, 1927 (Cestoda: Anoplocephalida). 608 41

Administration of N-hydroxy-2-acetylaminofluorene (90 mumol/kg, iv) to rats results in damage to periportal hepatocytes. The most prominent ultrastructural changes are the appearance of numerous unusual vesicles of about 200 nm diameter and the proliferation of the endoplasmic reticulum to form fingerprint-like structures. In order to characterize these vesicles and to investigate their possible origin, their enzymatic activity was studied by ultrastructural enzyme histochemistry. The vesicles as well as the fingerprint-like structures exhibited glucose-6-phosphatase activity. Continuities between the vesicles and the membranes of both the RER and the SER were frequently seen. The vesicles lacked ATPase, 5'nucleotidase and catalase activity. From these results we conclude that the vesicles may be an unusual proliferation of the endoplasmic reticulum.
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PMID:Genesis of unusual vesicles in rat periportal hepatocytes after administration of N-hydroxy-2-acetylaminofluorene. 614 30


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