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 activity level of acetylcholinesterase in the erythrocytes of 32 patients homozygous for sickle cell anemia was determined and compared with that of normal AA controls as well as with that of AS individuals. Acetylcholinesterase activity was markedly higher in erythrocyte membrane from SS individuals than in those from AS individuals or AA controls. Additionally, ATPase activities were also significantly higher in sickle cell erythrocytes as compared to normal cells. These higher values of acetylcholinesterase and ATPase activities in SS erythrocytes may be explained as a consequence of the abnormally high cation levels in sickle cell erythrocytes.
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PMID:Erythrocyte membrane enzymes in sickle cell anemia. 2. Acetylcholinesterase and ATPase activities. 214 41

Chlorpromazine, an antipsychotic drug, is found to inhibit Na+,K(+)-ATPase activity in rat brain microsomal membranes in vitro in concentration and time dependent manner but some inconsistency is observed when the effect was studied with respect to different temperatures. Various ligands and/or substrate affect the inhibition by chlorpromazine in different ways. The in vivo study with this drug shows that the activities of Na+,K(+)-ATPase, Ca2(+)-ATPase and acetylcholinesterase in the microsomal membranes of different organs are inhibit with increases in concentration or lengths of time of treatment and then levels off.
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PMID:The chlorpromazine inhibition of transport ATPase and acetylcholinesterase activities in the microsomal membranes of rat in vitro and in vivo. 216 37

Membranes obtained by lysis and Yeda-press treatment of synaptosomes (nerve endings) from calf brain cortex have been partitioned within the aqueous phases (and the interface between them) of a Ficoll-dextran-poly(ethylene glycol)-water two-phase system. By introducing the dye Procion yellow HE-3G in the upper phase, bound to poly(ethylene glycol), or in the lower phase, bound to dextran, the partition of the membranes could be strongly affected. The influence on the partition was more pronounced when the dye was bound to dextran. By using a number of two-phase systems in a counter-current distribution process, it was shown that the membrane preparation was inhomogeneous and that the fractions obtained differed in their contents of acetylcholinesterase, succinate dehydrogenase and ATPase. The affinity partitioning effect depended strongly on the concentration of polymer-bound dye. An optimum dye concentration was found when Procion yellow HE-3G was bound to poly(ethylene glycol). When the same dye was bound to dextran, the number of dye molecules per dextran molecule influenced the effectiveness of the extraction.
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PMID:Effect of dextran- and poly(ethylene glycol)-bound procion yellow HE-3G on the partition of membranes from calf brain synaptosomes within an aqueous two-phase system. 242 24

We have previously reported that Na+,K+-ATPase of nerve ending membranes is stimulated by catecholamines only in the presence of a brain soluble fraction. The filtration of this soluble fraction through Sephadex G-50 permitted the separation of two extracts of maximal UV absorbance (peaks I and II) which showed different effects on ATPases. Peak I stimulated both Na+, K+-ATPase and Mg2+-ATPase activities and peak II inhibited Na+, K+-ATPase activity. We have now studied the activity of ATPases in the presence of the whole eluate obtained from the Sephadex G-50 column. It was observed that maximal effects on ATPases were obtained with peaks I and II. Peak I and peak II fractions were unable to modify the activity of acetylcholinesterase or 5'-nucleotidase present in the synaptosomal membranes. The stimulatory effect of peak I on ATPases was concentration dependent (up to 1:100), it was stable at different pHs and it was reverted by catecholamines. The inhibitory effect of peak II on Na+,K+-ATPase was concentration dependent (up to 1:50,000), it was stable only at acid pH, and it was partially reverted by catecholamines. These findings indicate that the factors responsible for the effects of peaks I and II have different properties and that their actions on ATPases show enzyme specificity.
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PMID:Different properties of two brain extracts separated in Sephadex G-50 that modify synaptosomal ATPase activities. 245 36

The possible mechanism of the depressive effect of organic solvents on the central nervous system (CNS) was studied with synaptosome membranes as a model. The changes in the activities of the membrane-bound integral enzymes acetylcholinesterase, total adenosinetriphosphatase, and magnesium-activated adenosinetriphosphatase were determined after treatment with different concentrations of organic solvents in vitro. Aromatic hydrocarbons and chlorinated aliphatic hydrocarbons inhibited all the enzyme activities concentration dependently. Alcohols had no significant effect at the same dose levels. The results of the present study suggest that the CNS depressive effect of organic solvents may be based on their interaction with membrane integral proteins.
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PMID:Inhibition of synaptosome membrane-bound integral enzymes by organic solvents. 252 39

The localization of some enzyme in adult worms of Clonorchis sinensis was studied by histochemical method in this paper. Acid phosphatase was detected mainly in digestive duct, subtegument and the walls of testis, uterus and ovary; acetylcholinesterase was found in oral sucker, ventral sucker, pharynx; and ATPase was found to exist in oral sucker, ventral sucker, pharynx and muscle layer in the subtegument. The eggs of C. sinensis possessed the above three enzymes.
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PMID:[Histochemical studies on some enzymes in Clonorchis sinensis]. 252 40

Treatment of washed erythrocytes with tert-butyl hydroperoxide (0.5 mM, 10 min) inhibited basal Ca2+ + Mg2+-ATPase activity by 40% and calmodulin-stimulated activity by 54%. The inhibition was accompanied by the formation of methemoglobin and the aggregation of some membrane proteins into a high-molecular-weight polymer. Membranes, isolated from washed erythrocytes, showed a similar pattern of inhibition. Basal Ca2+ + Mg2+-ATPase activity was inhibited 50% at 10 min and 70% at 30 min while calmodulin-stimulated activity was inhibited 70% at 10 min and 84% at 30 min. Thiobarbituric acid-reactive products formed slowly during the first 10 min and then increased sharply between 10 and 30 min. The polymerization of membrane proteins was also observed during the tert-butyl hydroperoxide exposure. Inhibition of erythrocyte membrane enzymes was selective. The Na+ + K+-stimulated Mg2+ ATPase, like the Ca2+ + Mg2+-ATPase, was sensitive to membrane oxidation but the activities of Mg2+-ATPase and acetylcholinesterase were less inhibited by tert-butyl hydroperoxide. Acetylcholinterase was found to be very resistant to hydroperoxide treatment with less than 10% loss of activity. The effects of two other hyproperoxides on enzyme inhibition were studied also. Cumene hydroperoxide (0.5 mM) was found to be as potent as tert-butyl hydroperoxide but hydrogen peroxide at 10 mM did not produce thiobarbituric acid-reactive products or inhibit Ca2+ + Mg2+-ATPase activity until after 20 min. The selective effects of peroxides on these enzyme activities are discussed.
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PMID:Hydroperoxides selectively inhibit human erythrocyte membrane enzymes. 252 25

The activities of acetylcholinesterase and Ca2+ + Mg2+ ATPase were measured following treatment of human erythrocyte membranes with nonsolubilizing and solubilizing concentrations of Triton X-100. A concentration of 0.1% (v/v) Triton X-100 caused a significant inhibition of both enzymes. The inhibition appears to be caused by perturbations in the membrane induced by Triton X-100 incorporation. No acetylcholinesterase activity and little Ca2+ + Mg2+ ATPase activity were detected in the supernatant at 0.05% Triton X-100 although this same detergent concentration induced changes in the turbidity of the membrane suspension. Also, no inhibition of soluble acetylcholinesterase was observed over the entire detergent concentration range. The inhibition of these enzymes at 0.1% Triton X-100 was present over an eightfold range of membrane protein in the assay indicating an independence of the protein/detergent ratio. The losses in activities of these two enzymes could be prevented by either including phosphatidylserine in the Triton X-100 suspension or using Brij 96 which has the same polyoxyethylene polar head group but an oleyl hydrophobic tail instead of the p-tert-octylphenol group of Triton X-100. The results are discussed in regard to the differential recovery of enzyme activities over the entire detergent concentration range.
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PMID:The inhibitory effects of polyoxyethylene detergents on human erythrocyte acetylcholinesterase and Ca2+ + Mg2+ ATPase. 254 74

A decrease in total activity of ATPase and in specific activity of Na+,K+-ATPase as well as less rapid and distinct decrease in specific activity of acetylcholinesterase were observed in synaptosomal membrane after binding of bilirubin in vitro. Irradiation with blue light of the bilirubin-containing membrane particles caused a more distinct decrease in activity of these enzymes. Blood serum albumin, added to the suspension of bilirubin-containing particles of synaptosomal membrane, affected significantly the alterations in activity of membrane-bound enzymes caused by the irradiation. Character of the effect depended on pH of the medium and presence of organophilic ligands in blood serum albumin molecule.
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PMID:[Functional changes in the synaptic membrane during in vitro interaction with bilirubin and serum albumin]. 256 Aug 69

Synaptic membranes were isolated from 2 and 4-month-old rats, pair-fed controls (PF), prenatally (PAE) or pre + postnatally (PPAE) exposed to alcohol, and the activities of some membrane-bound enzymes were measured. We found a 22-36% reduction in the levels of the (Na + K)ATPase, Ca++ATPase, acetylcholinesterase and 5'-nucleotidase from PAE rats. This reduction was greater in PPAE animals. The transition temperature in Arrhenius plots of the synaptosomal (Na + K)ATPase activity from PPAE rats was lower than in control rat membranes, indicating an alteration of lipid-protein interactions. No change in transition temperature was noted in PAE animals. Also, there was a decreased cholesterol content in PPAE synaptic membranes, vs. controls, while there was no change in PAE membranes. Kinetic parameters of the synaptosomal (Na + K)ATPase from PPAE rats, revealed a decrease in the Km and Vmax for potassium. These findings indicate that prenatal alcohol exposure probably delays synaptic development, whereas continued alcohol exposure during lactation may, in addition, alter the physicochemical structure of synaptic membranes.
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PMID:Synaptic membrane alterations in rats exposed to alcohol. 282 96


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