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)

Very pure preparations of synaptic vesicles have been obtained from guinea pig cerebral cortex and from the electromotor synapses of Torpedo marmorata by density gradient centrifugation in a zonal rotor followed by chromatography on columns of glass beads of controlled pore size. Markers for soluble cytoplasm (lactate dehydrogenase), plasma and endoplasmic membranes membranes (Na-K-ATPase; acetylcholinesterase, NADPH-cytochrome c reductase], mitochondrial membranes [cytochrome oxidase] and lysosomes [acid phosphatase] were used to assess contamination and were undetectable. The only enzymes detected in the highly purified preparations from guinea pig cerebral cortex were Mg- and Ca-activated ATPases, but their content relative to acetylcholine fell on chromatography suggesting that they may be constituents of non-cholinergic vesicles. Lipids analyses of the highly purified vesicles confirmed earlier results and showed that glycolipids and lysolecithin are present in negligible amounts; this suggests that lysolecithin is not required for exocytosis of synaptic vesicles. A discussion of the probable limiting concentration of acetycholine in cerebral cortical vesicles derived solely from cholinergic terminals suggests that from 13 to 56% of the vesicles isolated are cholinergic, depending on the assumptions made.
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PMID:The preparation and characterization of synaptic vesicles of high purity. 13 27

The activities of several glycolytic enzymes (hexokinase, phosphofructokinase, pyruvate kinase, lactate dehydrogenase) as well as glycerol-1-phosphate dehydrogenase and (Mg2+)ATPase in normal cerebrospinal fluid (CSF) and blood plasma samples, from 12 healthy infants, aged 2-18 months, and in supernatants from brain tissue slices, taken during neurosurgical operations from infants of the same range of age were estimated. The values obtained confirm the high activity of the above enzymes found in animal brains, and indicate an independence of these activities in blood plasma and CSF. The origin of the activities of the investigated enzymes in CSF seems to be mainly, if not, exclusively, from brain tissue. This might be useful for detection of brain tissue damage as was earlier proven with LDH activity in CSF.
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PMID:Some glycolytic enzymes in normal cerebrospinal fluid, brain tissue and blood plasma of infants. 13 54

Skeletal muscles of flight rats showed no changes in the content of glycogen, adenosine triphosphatase activity of myosin and protein content in protein fractions (except the T fraction where the protein content increased on the 1st and returned to the normal on the 26th postflight day). On the 1st postflight day activities of aminotransferases and lactate dehydrogenase of sarcoplasmatic proteins were elevated and the isoenzyme spectrum of LDH was changed as if in muscular atrophy. The amount of free amino acids in muscles was lowered. On the 26 the postflight day the enzymic activity of sarcoplasmatic proteins remained increased whereas the isoenzyme spectrum of LDH returned to the normal and the amount of free amino acids grew significantly. In the microsomal fraction of muscles the phospholipid content decreased on the 1st and returned to the normal on the 26th postflight day.
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PMID:[Effect of a 22-day space flight on the metabolism of rat skeletal muscle tissue]. 13 80

No significant changes in the content of sarcoplasmatic and myofibrillar proteins were found in the myocardium of rats that made a 22-day flight onboard the biosatellite. On the 2nd and 26th postflight days the activity of aspartate and alanine aminotransferases of sarcoplasmatic proteins was increased and the total activity of lactate dehydrogenase and its isoenzyme spectrum remained unchanged. On the 2nd postflight day the ATPase activity of myosin of the myocardium was substantially lowered and on the 26th postflight day it returned to the normal. This decline in the ATPase activity of myosin can be regarded as an adaptive reaction to weightlessness.
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PMID:[Protein fractions and their enzyme activity in rat myocardium after a 22-hour space flight]. 13 82

A cell line (HGC-27) was established by culture of the metastatic lymph node from a gastric cancer patient diagnosed histologically as undifferentiated carcinoma. HGC-27 cells were polygonal or short spindle-shaped and adhered to glass surfaces as a monolayer. The cells were probably derived from gastric cancer cells, as their origin from mesenchymal tissues can be excluded morphologically and enzyme-histochemically. Enzyme activities were generally negative or low, except for adenosine triphosphatase, lactic dehydrogenase and leucine aminopeptidase. These scanty findings might reflect the undifferentiated character of the original tumor cells. The cloning efficiency was 5.3% in liquid medium and 1.0% in soft agar. The doubling time was about 17 hr. Chromosomal analysis revealed a mode of 109 and 110 chromosomes.
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PMID:Human cell line (HGC-27) derived from the metastatic lymph node of gastric cancer. 13 73

The effect of depersolone, of the oxygenation of the perfusing solution and of phenoxybenzamine pretreatment has been studied in the isolated rat liver intermittently perfused with a solution containing low molecular weight dextran at 4 degrees C. The use in liver preservation of Collins' C3-solution and of a special albumin-containing solution was tested. The behaviour of acid and alkaline phosphatase, esterase, lactate dehydrogenase and adenosine triphosphatase in the preserved liver was followed by means of histochemical methods allowing semi-quantitative evaluation. Pretreatment with phenoxybenzamine and perfusion by an albumin-containing solution reduced the lesion of the liver, while prednisolone and oxygenation of the perfusion solution improved preserving effect only moderately.
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PMID:Enzyme histochemical studies of the preserved rat liver. 14 May 69

Enzyme activity of adenosinetriphosphatase, NADH2-tetrazolium reductase and lactate dehydrogenase was studied in the rat perineurium 10, 20, 30, and 90 days post partum. The effect of under-nutrition was shown by a lack of enzyme activity in rats 30 days post partum in contrast to control animals, 30 days also corresponds to the time when, in normal rats, the perineurial diffusion barrier to exogenous macromolecules becomes established. In undernourished rats this diffusion barrier does not appear. At 90 days post partum raised enzyme activities indicate a high metabolic turnover in the perineurium even in animals with undernutrition.
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PMID:Impaired development of the rat perineurium by undernutrition. An enzyme histochemical study. 14 May 82

1. Homogenates of bovine pituitary neural lobe tissue were subjected to differential centrifugation. Six subcellular fractions (I-VI) were obtained and the distribution among them of various cell organelles was studied by means of markers. Fraction II (800-3000 gav), the nerve-ending fraction (neurosecretosomes), contained sedimentable lactate dehydrogenase, hormone and a large proportion of the total Mg2 + +Na+ +K+-ATPase. 2. Lysis of the neurosecretosomes in hypotonic sucrose solutions led to loss of lactate dehydrogenase and vasopressin. 3. Centrifugation of the granule fraction (IV) on a sucrose gradient (1.3-2.0 M sucrose) gave a bimodal distribution of vasopressin. Purified neurosecretory granules were recovered from the denser band. Centrifugation on modified gradients (0.8-2.0 or 0.4-2.0 M sucrose) increased the yield of hormone in the denser band but the purity of the granules was decreased. 4. Considerable purification of the neurosecretosomes (fraction II) was achieved by "washing". Centrifugation of washed neurosecretosomes on sucrose density gradients led to the accumulation of all activities at a region between 1.4 and 1.5 M sucrose. 5. The distribution of Mg2+ +Na+ +K+-ATPase in centrifugal fractions indicated that the neurosecretosomes had been isolated in relatively high yield.
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PMID:Subcellular fractionation by centrifugation of homogenates of the neural lobe of the bovine pituitary gland: identification of different pools of hormone in the homogenate and isolation of neurosecretosomes. 14 Nov 84

1. Homogenates of guinea-pig left ventricle were fractionated by differential pelleting and by centrifugation on continuous sucrose density gradients. 2. The principal subcellular organelles of myocardium, characterized by their marker enzyme content, were resolved by density gradient centrifugation in a small-volume zonal rotor. The equilibrium densities (p) of the principal organelles are (with marker enzymes in parentheses): sarcolemma, 1-12 (5'-nucleotidase); lysosomes, 1-16 (N-acetyl-beta-glucosaminidase); mitochondria, 1-17 (cytochrome oxidase); peroxisomes, 1-18 (catalase); cytosol (lactate dehydrogenase). 3. The subcellular distribution of various adenosine triphosphatase activities and previously unassigned enzymes was determined. Leucyl-beta-naphthylamidase and gamma-glutamyl transpeptidase showed both cytosol and sarcolemma components. Ca2+-dependent adenosine triphosphatase showed dual localization to the mitochondria and to the sarcolemma.
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PMID:Analytical subcellular fractionation of guinea-pig myocardium. 14 54

A rapid method for purifying Torpedo electric organ vesicles is described, which employs an isoosmotic continuous sucrose-glycine gradient followed by chromagography on CPG-10-3000 porous glass beads. The synaptic vesicles have a buoyant density of 1.057 g/ml. The purified vesicles are free of cholinesterase, lactate dehydrogenase and Na+, K+-stimulated ATPase activity. They contain a ouabaininsensitive, Na+, K+-inhibited, Mg2+, Ca2+-stimulated ATPase activity. This is further stimulated by acetylcholine but not by choline.
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PMID:Adenosine triphosphatase activity associated with purified cholinergic synaptic vesicles of Torpedo marmorata. 14 98


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