Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The plasma membtanes of normal rabbit endothelail cells were isolated by the use of an aqueous two-phase polymer system. The membrane fraction was identified by electron microscopy, and a fivefold to eightfold increase in the specific activity of two plasma membrane markers. Na+-K+-ATPase and 5'nucleotidase was found. Recovery of the enzyme markers averaged 45% and 22%, respectively. Analysis of the purified membranes for glucose-6-phosphatase, a marker for endoplasmic reticulum, showed no contamination by this structure. This method for cell membrane characterization is promising in determining the enzymatic alterations of diseased corneas.
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PMID:Isolation of the plasma membrane from corneal endothelial cells. 624 94

Kirk, Antonini, Weber and others have found that the activity of the specific phosphomonoesterase 5-nucleotidase is lowered. In the present study, carried out on male guinea pigs and fed with cholesterol for a period of 150 days, the authors discovered analogous change in 5-nucleotidase activity of the aortic wall. Administration of protein hydrolysate induced a statistically significant increase of the enzymic activity in the aorta of animals, fed with cholesterol. The combined treatment with protein hydrolysate and vitamins caused even more significant activation of the enzyme. The established changes in the activity of 5-nucleotidase were similar to the changes in the activity of adenylpyrophosphatase of animals under the same experimental conditions.
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PMID:[Effect of a protein hydrolysate on enzymatic activity in the aorta wall in experimental atherosclerosis]. 625 75

Differences in the pattern of the development of three enzymes of the plasma membrane have been established. The activity of Na, K-ATPase progressively increases, that of adenylate cyclase decreases, whereas the activity of 5-nucleotidase undergoes only slight changes during embryogenesis. Differences between these enzymes were also found with respect to the development of their sensitivity to the regulatory effects of catecholamines. Adrenaline reactivity of adenylate cyclase may be detected already in embryogenesis; it is lower than that in definite muscle tissue increasing during further ontogenesis. Catecholamine reactivity was not found in Na, K-ATPase and 5-nucleotidase up to the 17th day of incubation of chick embryos. The effect of adrenalin was observed at later stages of ontogenesis, it may be initiated by exogeneous cAMP and protein kinase. At postembryonic stages, similarity in the behavior of these enzymes was found with respect to the presence and pattern of their reaction to adrenalin (stimulation), as well as with respect to temporal dynamics of the effect. The data obtained indicate the existence of close connections between these enzymes, which are realized in the sequence adrenoreceptor-adenylate cyclase-cAMP-protein kinase-effector proteins.
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PMID:[Role of the hypothalamus and pituitary gland in the development of pancreatic islet sensitivity to glucose in fetal rats]. 626 78

Histoenzymological study of acid phosphatase (GP-AI), 5-nucleotidase (AMP-A), adenosine triphosphatase (ATP-A) and beta-galactosidase (GLAC-A) of the metencephalon of turtle shows a pattern of distribution of enzymes similar to amphibians and mammalian metencephalon which provides indication of homology of the nuclei and tracts such as nucleus raphe, nuclei cerebelli fasciculus longitudinalis medialis, commissura ansulata and internal arcuate fibers. The nerve fibers, tracts and commissures demonstrate strong activity of GLAC-A as demonstrated in frog and bat by the author in previous studies.
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PMID:Chemoarchitectonics of metencephalon of Testudo elegant. 626 93

It was investigated whether rat hepatocytes maintain their plasma membrane specialization (sinusoidal, lateral and bile canalicular sites) and their intracellular polarity (peribiliary region, rich in lysosomes and poor in mitochondria) after isolation. The morphology of the hepatocytes and the cytochemical localization of marker enzymes for the bile canalicular membrane (alkaline phosphatase, adenosine triphosphatase and 5' nucleotidase), for the lysosomes (acid phosphatase) and for the mitochondria (beta-hydroxybutyrate dehydrogenase and succinate dehydrogenase) were studied in situ and directly after isolation using both light and electron microscopy. The morphology of the cells and the cytochemical activity of acid phosphatase, succinate dehydrogenase and beta-hydroxybutyrate dehydrogenase showed that in isolated cells, as in situ, the lysosomes were concentrated in bands, devoid of mitochondria. Unlike in situ the reaction product of alkaline phosphatase, adenosine triphosphatase and 5'nucleotidase was evenly distributed along the entire plasma membrane of the isolated cells. Morphologically, no tight or gap junctions or desmosomes could be detected in the isolated cells, while the plasma membrane appeared to be homogeneously covered with uniform microvilli. In conclusion it can be stated that during isolation the hepatocytes loose their distinct plasma membrane specialization, but maintain their peribiliary region rich in lysosomes and poor in mitochondria.
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PMID:Plasma membrane specialization and intracellular polarity of freshly isolated rat hepatocytes. 627 81

The contribution presented deals with the distribution of adenosine triphosphatase (ATP-A) and 5-nucleotidase (AMP-A) in the spinal cord and medulla oblongata of hedgehog. The highlights of this study are: (1) AMP-A activity is stronger in neuropil than in neurons, in all the areas of spinal cord and medulla oblongata. In the nerve cells the enzyme is localized at the peripheries of the neurons, whereas the cytoplasm and nuclei are completely free from enzymatic activity. Reaction in blood vessels is quite high both in gray and white matter. (2) ATP-A activity is seen mainly at the peripheries of the neurons. The neuropil activity varies from mild to intense. Reaction in blood vessels is quite strong in all the areas. (3) Fibrous bundles and tracts are negative for both the enzymes. (4) In general, the activity of ATP-A and AMP-A is strongest in cranial nerve nuclei, irrespective of their sensory or motor nature. The distribution of these enzymes has been correlated with the functions of various nuclei of spinal cord and medulla oblongata in hedgehog, and compared with other mammals.
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PMID:Histoenzmological mapping of ATPase and 5-nucleotidase in the spinal cord and medulla oblongata of hedgehog (Paraechinus micropus). 628 Apr 49

Semm's technique of endocoagulation has been used by the authors for haemostasis in endoscopic abdominal surgery at the Department of Gynecology and Obstetrics, University of Kiel since 1973. --Enzyme-histochemical and histological tests, all based on endocoagulation or high-frequency current procedures, were applied to 100 human fallopian tubes. Fifteen of them remained uncoagulated and were used for comparison. --Membrane ATPase, 5-nucleotidase, cytochrome-C-oxydase, and other essential enzymes in cellular metabolism were inactivated by temperatures in excess of 57 degrees C. These enzymes, consequently, were no longer detectable from enzyme-histochemical preparations, whereas active tissue regions, those which still contained vital cells, were stained black to brown. --Negative enzyme reactions occurred in response to a coagulation forceps temperature of 120 degrees C, when applied not less than 20 seconds. Residual enzyme activities were still recordable from certain tubal areas, when forceps temperatures below 120 degrees C had been used. In such cases coagulation was insufficient, particularly in the inner layers of tubes (epithelium, mucosa). Temperatures above 130 degrees C and coagulation lengths of more than 20 seconds proved to be unnecessary, since no improvement in results was thus achievable. Temperatures of 140 degrees C and more have changed coagulated tissue into "adhesive" and make it stick to the coagulation forceps. Instrument withdrawal can in such cases cause bleeding rather than the desired haemostatic effect.
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PMID:[Devitalization and haemostasis by thermal destruction--results of enzyme-histochemical and histological examination of oviduct specimens, following tissue coagulation by means of endocoagulation or high-frequency current (author's transl)]. 628 61

Rats exposed to cosmetic kerosene mists (odourless kerosene), concentration of 75 and 300 mg/m3 for 14 days, underwent morphological and cytoenzymatic liver tests and biochemical tests of lipids composition in this organ. In addition, lipids concentration and activity of test--enzymes in blood serum were determined. The findings were: passive congestion, fine--droplet fatty degeneration in I zones of clusters and increased number of Browicz--Kupffer's phagocytes near liver triads. Those changes were accompanied by: decreased activity of succinic dehydrogenese (SDH), tetrazolic NADPH--reductase (NADPH-r.t.) and glucose-6-phosphatase (G-6-P-ase) and increased activity of adenosine triphosphatase (Mg++-ATP-ase) and acid phosphatase (AcP). In blood serum medium increase of base phosphatase (AP), 5-nucleotidase (5-Nt) and leucyloaminepeptidase (LAP) and decreased activity of prothrombin (Pt) were found. In addition, it was demonstrated that liver steatosis was characterized by cumulation of free fatty acids, phospholipids and cholesterol esters with simultaneous decrease in triglycerides content in this organ. The obtained results indicate that changes induced by kerosene hydrocarbons in liver are focal and cumulate in I zones of liver clusters. The degree of lesion varies with the extent of exposure, and results from toxic effects of this preparation on hepatic cells lypoproteid membranes.
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PMID:[Comparative studies on the toxicity of various dieelectrics, kerosene derivatives, used in the electroerosion technic. I. Morphological, cytoenzymatic and biochemical changes in the liver of rats chronically exposed to kerosene hydrocarbons]. 630 48

Thermal inactivation studies performed with several membrane-bound enzymes such as chitin synthase, cytochrome c oxidase, nucleotidase, as well as bacterial, mitochondrial and plasma membrane ATPases from yeast in H2O and 2H2O indicated that most of these enzymes could not be protected by 2H2O against thermal inactivation. Only the Escherichia coli ATPase, which is located at the surface of the membrane, and the cytochrome c oxidase were stabilized by heavy water.
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PMID:Does 2H2O also protect membrane-bound enzymes? 630 84

Acid phosphatase, alkaline phosphatase, glucose-6-phosphatase, Mg-activated adenosine triphosphatase and 5'nucleotidase were demonstrated in the rat liver using a cerium-based method. This method can be applied routinely and yields better results than the lead-based method. The tissue was postfixed in osmium tetroxide and potassium ferrocyanide which considerably enhances the membrane contrast in comparison with solely osmium tetroxide postfixation. This facilitates the precise localization of the reaction product.
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PMID:Cytochemical demonstration of phosphatases in the rat liver by a cerium-based method in combination with osmium tetroxide and potassium ferrocyanide postfixation. 630 35


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