Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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

Histochemical localization of acetylcholinesterase and butyrylcholinesterase in the salivary glands has unfolded the significant fact that salivary glands are of two types, one being enzymatically negative and the other showing positive activity. Activity of these enzymes has been linked with the operation of glandular dynamics, particularly concerning the synthetic and secretory processes. The enzymes have been seen localized in the core of jaw. Contrary to it they are absent in the papillary and interpapillary zones of the jaw. Absence of esterases in the papillary and interpapillary ductules has been correlated with its possible non-involvement in the synthesis of vasodilating and anticoagulating materials. The experiments on effect of biting on host tissue give a faint indication of vascular dilation due to bite. Likewise, experiments on enzymatic state of a salivary gland after leech-bite reveal that the diminution of the reactive coverage area in the salivary glands reaches its maximum in the case of ATPase, indicating thereby its more involvement in salivary functions than those of esterases and acid phosphatase.
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PMID:Studies on the host-parasite interaction and role of esterases during biting of the Indian cattle leech, Poecilobdella granulosa. 13 92

The influence of cholesterol on the membrane-bound acetylcholinesterase and (Ca2+ + Mg2+)-ATPase was studied in erythrocytes of five groups of male rats fed different fat-supplemented diets. Two groups of rats were fed essential fatty acid (EFA) sufficient diets with 5% lard or corn oil as the dietary fat, and two groups were fed EFA-deficient diets: a basic, fat-free diet and the same diet supplemented with 5% hydrogenated beef fat. One additional group of rats was fed a stock diet. The kinetic changes recorded were in the degree of the cooperativity of the inhibition by F- of the acetylcholinesterase and the activation by Ca2+, and by Mg2+ of the (Ca2+ + Mg2+)-ATPase. The kinetic behavior of the enzymes was only modified by cholesterol feeding when they were bound to a membrane with a high fatty acid fluidity (e.g. derived from rats fed the corn oil-supplemented diet). The enzymes from a membrane with a low fatty acid fluidity (e.g. derived from rats fed a lard-supplemented diet) were not altered by cholesterol feeding. The changes were noticeable after 24 hours of cholesterol feeding. It is suggested that the in vivo cholesterol sites are involved in a regulatory mechanism for mammalian membrane-bound enzymes.
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PMID:Kinetic modifications of the acetylcholinesterase and (Ca2+ + Mg2+)-ATPase in rat erythrocytes by cholesterol feeding. 13 2

Nerve cell bodies, large and multipolar, were isolated in bulk with the least possible contamination from the pig brain stem. The activities of two neurobiologically important membrane enzymes, Na+, K+-ATPase, and acetylcholinesterase, in the isolated cell bodies were estimated. Na+, K+-ATPase [EC 3.6.1.4], more accurately called ouabain-sensitive ATPase of the nerve cell body, hydrolyzed 94 micronmoles of ATP per h per 100 mg of protein. This activity was one-fourth that in the brain stem. Nerve cell bodies contained a large amount of Ca2+, 275 micronmoles per 100 mg of protein, about half of which was calculated to exist as compounds other than calcium orthophosphate. However, the Na+, K+-ATPase of the nerve cell bodies was not stimulated by EGTA, in contrast to that of the brain stem. Acetylcholinesterase [EC 3.1.1.7] and cholinesterase [EC 3.1.1.8] activities were estimated separately by the use of the specific inhibitors Persidol and BW 284C51 dibromide. Acetylcholinesterase was almost completely responsible for the hydrolysis of acetylcholine in the nerve cell bodies isolated from the brain stem and little cholinesterase activity was detected. 1300-1400 micronmoles of acetylcholine was hydrolyzed per h per 100 mg of protein of the neuronal cell bodies; this activity was about four times higher than that in the brain stem. The differences between the specific activities of Na+, K+-ATPase, and acetylcholinesterase in theneuronal cell bodies and the brain stem are discussed in the light of electron microscopic analysis of the distribution of these enzymes and the preservation of the plasma membrane of the isolated cell bodies.
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PMID:Biochemical characterization of the neuron. ATPase and acetylcholinesterase activities of neuronal cell bodies isolated in bulk from the pig brain stem. 14 Aug 66

The thoracic muscles of Drosophila melanogaster can be classified into two classes, the fibrillar and the tubular muscles, on morphological grounds. Histochemical techniques were used to characterize these two classes of muscle according to their content of various enzymes (alpha-glycerophosphate, NAD-dependent isocitrate, malate and succinate dehydrogenases, fumarase, acid phosphatase, adenosine triphosphatase and acetylcholinesterase) and of glycogen. These investigations showed that the two muslces types are histochemically very different and, further, that the morphologically similar tubular muscles are heterogeneous with respect to their enzyme content. In particular, the tergal depressor of the trochanter of the second leg, the largest of the tubular muslces, has considerably less of all the enzymes studied, with the exception of acetylcholinesterase, than all the other tubular muscles examined. The histochemical techniqes were also used to follow the changes in enzyme levels that occur during development of the indirect flight muscle fibres. All the enzymes that are present in adult flight muslces showed an increase in staining intensity throughout muscle development. Some minor differences were observed in the time of appearance and rate of increase of intensity of the different enzymes.
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PMID:A histochemical study of the muscles of Drosophila melanogaster. 14 43

A defective membrane mechanism has been suggested [Arch. Neurol. 33, 315 (1976)] for the pathogenesis of Duchenne muscular dystrophy. The characteristic clinical and biological findings, including leakage of cellular enzymes into the serum in the disease, have been duplicated by the imipramine/serotonin rat myopathy model. Sarcolemma was prepared from quadriceps femoris muscles of control and myopathy-affected animals. The activities of sarcolemmal adenosinetriphosphatase and acetylcholinesterase were inhibited in vitro by imipramine and serotonin. The inhibition by imipramine of these sarcolemma-bound enzyme systems decreased the Vmax and increased the Km. This mixed type of inhibition is consistent with an imipramine-induced interference at these enzyme sites and a disruption of lipid-protein interrelations. We hypothesize that such conformational membrane changes might contribute to the leakage of macromolecules such as enzymes from the cell interior.
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PMID:Mechanisms of cellular enzyme release. II. Inhibition of sarcolemmal enzymes by myopathy-inducing agents. 14 73

Human erythrocytes from healthy male donors were fractionated with respect to in vivo age by simple centrifugation in order to characterize changes in the functional integrity of the membrane during the life-span of the cell. The three enzymes, Na/K-ATPase, glyceraldehyde-3-phosphate dehydrogenase and NADH-ferricyanide reductase, were found not to change with age, but significant age-dependent decreases were observed in the cases of acetylcholinesterase, phosphoglycerate kinase, purine nucleoside phosphorylase, adenylate kinase, Mg-ATPase and alkaline phosphatase. The possibility that these changes were attributable to mechanisms other than age-related inactivation, such as reticulocyte contamination, differential resealing and crypticity, was investigated. Only the decrease in acetylcholinesterase could be explained wholly in terms of reticulocyte contamination. A decrease in membrane integrity on ageing was observed, which accounted for approximately half the change in alkaline phosphatase and may have contributed to the other enzyme activity changes. This membrane integrity effect masked a real decrease in the highly cryptic NADH-ferricyanide reductase, this decrease being apparent only after total disaggregation of the membrane with nonionic surfactant.
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PMID:Changes in the activities of some membrane-associated enzymes during in vivo ageing of the normal human erythrocyte. 14 40

The residual effects of dihydroergotoxine mesylate (DHET: active substance of Hydergine), ethanol, and DHET + ethanol were investigated in aging male mice. Prolonged alcohol or DHET consumption was found to prolong hexobarbital sleeping time and increase oxygen consumption. Administration of alcohol combined with DHET inhibited the ability of each drug to prolong hexobarbital sleeping time and increase oxygen consumption. There were no significant differences between groups in forebrain synaptosomal (Na+-K+) adenosine- triphosphatase and acetylcholinesterase activity or cerebellar protein, DNA and RNA content. The relative proportion of phospholipid to protein in isolated myelin of the medulla was significantly reduced, whereas the sphingomyelin content of total phospholipid was highest in alcohol-treated mice. Conocomitant treatment of mice with alcohol combined with DHET prevented the physiological and neurochemical changes caused by alcohol and, in some cases, DHET, administered alone.
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PMID:Dihydroergotoxine and ethanol: physiological and neurochemical variables in male mice. 14 92

Red blood cell plasma membranes contain a number of enzymes: ATPases, anion transport protein, glyceraldehyde 3-phosphate dehydrogenase, protein kinases, adenylate cyclase, acetylcholinesterase. Most of them are tightly bound to the membrane and are present in small amounts. As a result, structural characterization of erythrocyte membrane enzymes has not yet been successful. Functional studies have, however, yielded a great deal of information. ATPases allow active transport of cations (calcium, sodium, potassium). Anion transport protein controls movements of chloride and phosphate ions, and of glucose and water. Among glycolytic enzymes: glyceraldehyde 3-phosphate dehydrogenase is partially bound to the membrane. Protein kinases catalyze the phosphorylation of several membrane proteins, one of which (spectrin) is involved in red blood cell mechanical properties. The physiological role of adenylate cyclase is unknown. Acetylcholinesterase is an ectoenzyme. Calcium-dependent ATPase, adenylate cyclase and phosphorylation of erythrocyte membrane proteins have been found abnormal in various conditions: hereditary spherocytosis, sickle-cell anemia, progressive muscular dystrophies, all of these disorders being associated with a decreased deformability of the erythrocyte.
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PMID:The enzymes of the red blood cell plasma membrane. 14 25

Rat muscle nerves were examined histochemically for their activity of acetylcholinesterase (AChE). The corresponding muscles were stained for myofibrillar ATPase and for NADH diaphorase. The nerves to the extensor digitorum longus (EDL) muscle and to the medial head of the gastrocnemius (MG) muscle consist of a motor axons of high AChE activity. Both muscles are characterized by the prevalence of type II muscle fibres. On the other hand, the soleus muscle and the quandratus femoris muscle, both mainly composed of type I muscle fibres, are innervated by a motor axons of low AChE activity. Since it is well established that EDL and MG are typical fast-twitch muscles and that the soleus, and probably also the auadratus femoris, is a typical slow-twitch muscle, it is suggested that, in rat, fast muscles are innervated by motor nerve fibres of high AChE activity and slow muscles are innervated by motor axons of low AChE activity.
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PMID:Acetylcholinesterase activity in motor nerve fibres in correlation to muscle fibre types in rat. 14 38


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