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)

We have established the suitability of adenosine 5'-O-(gamma-thio)triphosphate(ATP gamma S) as an analog of ATP for the nucleoside triphosphatase activity of Escherichia coli transcription termination protein rho (EC 3.6.1.3). Steady-state analysis gives a Vmax of 1.5 mumol min-1 mg-1, 9% of the value with MgATP as substrate, and indicates that ATP gamma S binds as tightly (based on Km and Ki versus ATP) to rho as does ATP. (gamma-S)[beta gamma-17O,gamma-17O,gamma-18O]ATP gamma S was used as substrate to produce chiral product inorganic [17O,18O]thiophosphate and determine the stereochemical course of the hydrolysis. The results of this determination, inversion at the thiophosphoryl phosphorus, indicate that the enzymatic hydrolysis of ATP by rho consists of a direct transfer of the phospho group to water without the existence of a phosphoenzyme or phospho-RNA intermediate.
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PMID:Absence of a phosphorylated intermediate during ATP hydrolysis by Escherichia coli transcription termination protein rho. 353 18

X-ray microanalysis of single muscle fibres visualized in the electron microscope has been applied to human muscle biopsies to quantify changes of intracellular elements after knee-surgery with subsequent immobilization for 6 weeks. An increase of intracellular chlorine (Cl; P less than 0.001) and of sodium (Na; P less than 0.1) concentrations were found 1 and 6 weeks post-surgery. Intracellular potassium (K), phosphorus and sulphur concentrations were not significantly changed. The increased Cl and Na concentrations may be an indication of a decreased activity of the ATPase-dependent Na/K-pump in the sarcolemma and/or of an increased sarcolemmal permeability for Na and Cl.
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PMID:Changes in elemental composition of human muscle fibres following surgery and immobilization. An X-ray microanalytical study. 363 Jul 25

Previous work has demonstrated that myocardial ischemia results in a breakdown of the excitation-contraction coupling system of cardiac muscle associated with lysosomal activation. It has been hypothesized that lysosomal activation during the course of myocardial ischemia is mediated by the production of oxygen free radicals. We have tested the hypothesis that myocardial ischemia results in the activation of lysosomal phospholipase C and disruption of calcium transport in sarcoplasmic reticulum (SR) mediated by oxygen free radicals. Three groups of dogs were studied: sham-operated controls (n = 6); normothermic global ischemia of 30-min duration (n = 6); and 30 min of normothermic global ischemia pretreated with intracoronary superoxide dismutase (SOD, 10 micrograms/ml) plus catalase (25 micrograms/ml). In vitro, isolated SR demonstrated a significant depression of calcium uptake rates and Ca2+-stimulated, Mg2+-dependent ATPase activity at both pH 7.0 and 6.4 with the depression at pH 6.4 greater than 7.0. This depression of SR function was significantly inhibited in hearts pretreated with SOD plus catalase. In sham-operated controls, acid-induced dysfunction was associated with substantial loss of phospholipid phosphorus and major changes in phospholipid composition. SR contained an extremely active, ion-independent sphingomyelinase-phospholipase C (SM-PLC) that had maximal activity at pH 4.5-5.0. This SM-PLC was activated when control SR was incubated at acid pH and the specific activity of SM-PLC was decreased 50% in SR isolated from normothermic global ischemia. Activity remained at control levels in hearts pretreated with SOD plus catalase.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Sarcoplasmic reticulum dysfunction: phospholipid alterations induced by lysosomal phospholipase C. 377 91

A new procedure for the rapid isolation of renal cortical brush-border and basolateral membranes from the same homogenate is described. Brush-border membranes isolated using Mg2+-EGTA precipitation were enriched 18-fold for leucine aminopeptidase and had a recovery of 32.5%. Basolateral membrane fractions were isolated using a discontinuous sucrose gradient and showed an enrichment of 10.7-fold and recovery of 12.8% using (Na+,K+)-ATPase as a marker enzyme. Lipid analysis using two-dimensional TLC separation of phospholipids and gas liquid chromatography for cholesterol showed marked differences in the lipid composition of the brush-border and basolateral membranes. The brush-border membrane had increased sphingomyelin, phosphatidylserine, ethanolamine plasmalogens, and an increased cholesterol-to-phospholipid and sphingomyelin-to-phosphatidylcholine ratio compared to the basolateral membrane. The relative turnover of total membrane and individual phospholipid species using a double isotope ratio method was carried out. Phospholipids were labeled with either phosphorus 32 and 33 or acetate (3H, 1-14C). The relative turnover of phospholipid species and cholesterol differed strikingly. Phosphatidylcholine showed a high turnover, phosphatidylethanolamine and phosphatidylinositol had intermediate values and sphingomyelin, phosphatidylserine and cholesterol had low relative turnover rates. The order of phospholipid class relative turnover was independent of the labeled precursor used. The brush-border membrane had a significantly reduced relative turnover rate for total membrane phospholipids, sphingomyelin and cholesterol compared to the basolateral membrane. These data show marked differences in the lipid composition and relative turnover rates of the phospholipid species of the brush-border and basolateral membranes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Renal cortical brush-border and basolateral membranes: cholesterol and phospholipid composition and relative turnover. 399 20

Mitochondria from brown adipose tissue of cold-acclimated rats (6 degrees C) oxidize alpha-ketoglutarate at a rate twice that of controls (26 degrees C). In both groups, however, the phosphorus: oxygen ratio with alpha-ketoglutarate never exceeded unity, and it is essentially zero with either succinate or alpha-glycerophosphate. Adenosine triphosphatase activity of these mitochondria is very low and it is not stimulated by 2,4-dinitrophenol. In addition, both respiration and phosphorylation are unaffected by adenosine diphosphate, 2,4-dinitrophenol, bovine serum albumin, or glutathione. Endogenous respiration of tissue slices is not stimulated by 2-4-dinitrophenol. It is suggested that brown fat mitochondria are not capable of oxidative phosphorylation, but do phosphorylate at the substrate level. Since these findings provide an unusual example of electron transport by means of an energetically nonconservative pathway, their significance to thermogenesis by brown adipose tissue is particularly emphasized.
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PMID:Nonphosphorylating respiration of mitochondria from brown adipose tissue of rats. 422 65

Tritiated H(3)-digoxin specifically binds to a cardiac (Na(+) + K(+))-activated adenosine triphosphatase. In the presence of adenosine triphosphate and other nucleoside di- and triphosphates, binding is stimulated by sodium ion, the apparent rate constant being similar to that reported for phosphorus-32 incorporation from adenosine triphosphate and for the adenosine triphosphatase activity. In the presence of magnesium, manganese, inorganic phosphate, or other ions, sodium ion inhibits binding. The data support an allosteric type of sodium-potassium ion pump.
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PMID:Tritiated digoxin binding to (Na+ + K+)-activated adenosine triphosphatase: possible allosteric site. 423 May 10

The preparation of cytoplasmic membranes from suspensions of Staphylococcus aureus lysed by an enzyme recently isolated in these laboratories is described. These membranes contained: protein, 34.4%; ribonucleic acid, 6.6%; lipids, 34.5%; and total phosphorus, 1.4%. Such membranes exhibited adenosine 5'-triphosphatase (E.C. 3.6.1.3) activity, liberating orthophosphate at an initial rate of 0.53 mumole per min per mg of protein under optimal conditions. The enzyme was Mg(++)-dependent and K(+)- or Na(+)-stimulated. Maximal activity was observed with a molar adenosine 5'-triphosphate (ATP) to Mg(++) ratio of 1. One mole of orthophosphate was liberated per mole of ATP; the other product of digestion was adenosine 5'-diphosphate. Inorganic pyrophosphate and the 5'-triphosphates of guanosine, uridine, and cytidine were also attacked by membrane preparations, but more slowly than ATP. Ouabain, p-chloromercuribenzoate, and 2,4-dinitrophenol did not alter adenosine triphosphatase activity, whereas both Atebrine and chlorpromazine were inhibitory.
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PMID:Adenosine triphosphatase in isolated membranes of Staphylococcus aureus. 423 Aug 57

A microsomal adenosine triphosphatase (ATPase) that requires both sodium and potassium ions is thought to be identical with, or an integral part of, the active cation transport system located in cell membranes. Attempts to isolate and purify (Na(+) + K(+))-ATPase have met with limited success because solubilization of microsomal protein causes partial, if not complete, loss of enzymatic activity. We now report the isolation from rat kidney microsomes of proteins which, though enzymatically inactive, could still be identified as components of the (Na(+) + K(+))-ATPase system. Phosphoproteins known to be intermediates in the hydrolysis of ATP by (Na(+) + K(+))-ATPase were prepared by incubating rat kidney microsomes with gamma-labeled ATP(33) in the presence of sodium or with P(32)-orthophosphate in the presence of ouabain. After the P(32)- and P(33)-labeled microsomes had been dissolved in phenol-acetic acid-urea, the resultant solutions were mixed and subjected to polyacrylamide gel electrophoresis. The radioactivity from both phosphorus isotopes was found almost exclusively in one of the resultant 21 protein bands. In contrast, the radioactive protein from DFP(32)-labeled microsomes moved slightly faster than the radioactive protein from microsomes labeled with P(33)-orthophosphate in the presence of ouabain. DFP inhibits (Na(+) + K(+))-ATPase by reacting with a nucleophilic site at or near the active site. These results suggest that while a single protein component of (Na(+) + K(+))-ATPase accepts the terminal phosphate from ATP, the final splitting of this phosphoprotein intermediate may be catalyzed by nucleophilic sites on a second protein.
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PMID:Identification of components of (Na+ plus K+)-adenosine triphosphatase by double isotopic labeling and electrophoresis. 424 29

1. The composition of a vesicular cell-membrane fraction from leucocytes has been studied. The bulk of the mass is accounted for as protein and lipid. A small amount of carbohydrate, including some N-acetylneuraminic acid, is present. The phospholipid/cholesterol molar ratio is 1.4 and differs from that for the whole cell. 2. Labile phosphorus groups are present in the membrane but the analysis is complicated by the presence of phosphorus occluded in the membrane vesicles. 3. Leucocidin does not change the gross composition of the membranes or alter the amount or reactivity of the phosphorus compounds. 4. The cell-membrane fraction has considerable avidity for an impurity present in commercial [(32)P]orthophosphate. When this is removed [(32)P]orthophosphate or [(32)P]ATP does not label the membrane. 5. The presence of an NADH(2)-cytochrome c oxidoreductase and an alkaline phosphatase is described. The adenosine-triphosphatase activity of the membrane has not been found to depend on the presence of Na(+) or K(+).
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PMID:Composition and properties of a cell-membrane fraction from the polymorphonuclear leucocyte. 428 73

Protoplasts of Listeria monocytogenes strain 42 were fractionated after control lysis on a Ficoll (a polysucrose) density gradient. Visually, five zones could be recognized in the gradient. The first one was composed of amorphous cytoplasmic solutes (fraction 1a) and a mixture of particles (fraction 1b). These were: (i) light particles that were lipase-sensitive and composed of six subunits and (ii) heavy particles, sensitive to ribonuclease and devoid of fine structure. The second zone consisted of tubules and vesicles still harboring cytoplasmic components (fraction 2), whereas the third zone contained only empty vesicles and protoplast ghosts (fraction 3). The material congregating into the fourth zone was morphologically identical to that of the third (fraction 3a). The fifth and heaviest zone contained a mixture of (i) particles without any substructure and (ii) partly lysed protoplasts (fraction 4). Fractions 1b and 4 were the richest in nucleic acids (ribonucleic acid, 11.4 and 9.4%, respectively; deoxyribonucleic acid, 5.1 and 4.8%, respectively), whereas fraction 1b had the highest protein contents (74.6%). Phospholipids were mainly found in fractions 2 and 3. Except for fraction 1, all materials contained significant amounts of protein-bound phosphorus. The main concentrations of four enzymes were: glucose-6-phosphate dehydrogenase (fraction 1a); adenosine triphosphatase and reduced nicotinamide adenine diphosphate oxidase (fraction 3); nitro blue tetrazolium chloride reductase (fraction 2). Fractionation of strain 42 after addition of (32)P during the mid-log phase of growth revealed that the radio-activity was mainly detected in fraction 1b, when growth in the presence of the marker was allowed for 10 min, and in fraction 2, when growth was allowed for 90 min. The vesicles of fraction 2, often tubular, are probably of mesosomal origin, whereas those of fraction 3, which are always spherical, represent, most likely, the bulk of the cell plasma membrane. Our data showed slight chemical differences between these two fractions, but the differences in enzymatic activities and lipid-phosphorus incorporation during long pulse experiments were most dramatic.
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PMID:Fractionation and characterization of the plasma and mesosome membrane of Listeria monocytogenes. 430 41


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