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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The chemical properties of two highly purified preparations of (sodium + potassium)-activated adenosine triphosphatase (NaK ATPase) and their subunits have been compared. One preparation is derived from the rectal gland of the spiny dogfish shark, Squalus acanthias and the other preparation is derived from the electric organ of the electric eel, Electrophorus electricus. Ouabain binding and phosphorylation from [gamma-32-P]ATP for both enzymes ranged from 4000 to 4300 pmol per mg of protein. This gives a stoichiometry for ouabain binding and phosphorylation of 1:1 for both enzymes. The molar ratios of catalytic subunit to glycoprotein was 2:1 for both enzymes, suggesting a minimum molecular weight of 250, 000, which agrees with the molecular weight obtained by radiation inactivation. Assuming that only one of the two catalytic subunits is phosphorylated and binds ouabain per (sodium + potassium)-activated adenosine triphosphatase molecule the data on phosphorylation and ouabain binding also give a molecular weight of 250, 000. The data on phosphorylatiion, ouabain binding, subunit composition, and molecular weight based on radiaion inactivation are thus all internally consistent. A technique has been developed for isolation of pure catalytic subunit and glycoprotein in good yields by preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A variety of chemical studies have been carried out with the purified subunits. The amino acid composition of the catalytic subunit was different from that of the glycoprotein, but the amino acid composition of each of the two subunits was essentially the same for both species. However, the NH2-terminal amino acid for the catalytic subunit was alanine for the rectal gland enzyme and serine for the electric organ enzyme, suggesting some differencesin amino acid sequences for the two species. The NH2-terminal amino acid for the glycoprotein was alanine for the two species. The glycoproteins from both species contained the same carbohydrates but in quite differing amounts. The carbohydrates were glucosamine, sialic acid, fucose, galactose, mannose, and glucose. The release of all the sialic acid from the electric organ enzyme and the release of 40% of the sialic acid from the rectal gland enzyme did not affect (sodium + potassium)-activated adenosine triphosphatase activity. Both enzymes contained the following phospholipids, which accounted for 98 to 100% of the total phospholipid phosphorus: sphingomyelin, lecithin, phosphatidylserine, phosphatidylethanolamine, and phosphatidylinositol. With the exception of phosphatidylethanolamine, and phosphatidylinositol. With the exception of phosphatidylserine, the amount of any phospholipid per mg of enzyme as well as the total phospholipid content were quite different for the two enzymes.
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PMID:Molecular properties of purified (sodium + potassium)-activated adenosine triphosphatases and their subunits from the rectal gland of Squalus acanthias and the electric organ of Electrophorus electricus. 12 22

A Mg2+- and Ca2+-stimulated adenosine triphosphatase (ATPase) at the outer surface of intact Ehrlich ascites tumor cells is described. A surface-bound adenosine triphosphate (ATP)-splitting activity at a lower rate was also demonstrated in the absence of Ca2+ but with Mg2+, Na+, and K+ present in the isotonic medium. Hence, when part of the Mg2+ was exchanged for Ca2+, a marked increase of the ATP-splitting activity was observed. The stimulatory effect of Ca2+ was seen only if both Na+ and K+ were present in the isotonic incubation medium. Thus, the enzyme activity was Mg2+- and Ca2+-dependent. Ca2+, together with the monovalent cations was inhibitory compared with Mg2+ under similar conditions. The apparent Km for ATP for the Mg2+-stimulated ATPase is 0.05 mM, while that of the Mg2+- and Ca2+-stimulated enzyme is 0.10 mM. The Vmax of the former is 0.8 mu-mole per 100 mg Schneider protein per 30 sec compared with 1.92 mu-moles per 100 mg Schneider protein per 30 sec for the latter. The calculated Km for the Mg2+- and Ca2+-stimulated ATPase after subtraction of the Mg2+-stimulated part is 0.22 mM. Ethacrynic acid and N-ethylmaleimide both inhibited the Mg2+- and Ca2+-stimulated ATPase by about 10 percent, while the ouabain inhibition was 15 percent. Cytochalasin B did not influence the enzyme activity, whereas La3+ had a slight stimulatory effect.
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PMID:A Mg2+- and Ca2+-stimulated adenosine triphosphatase at the outer surface of Ehrlich ascites tumor cells. 12 5

Cytochalasin A at 10-20 mug/ml inhibits growth and sugar uptake by Saccharomyces strain 1016. The effects of cytochalasin A in intact cells were completely prevented when 1 mM cysteine or dithiothreitol was added along with cytochalasin A, but were not eliminated by thiols added after inhibition had occurred. Purified yeast hexokinase, glucose-6-P dehydrogenase, phosphofructokinase and aldolase were not sensitive to cytochalasin A (20 mug/ml). Glyceraldehyde-3-P dehydrogenase was strongly inhibited by cytochalasin A (5 mug/ml); activity was promptly restored by thiols. Anaerobic glycolysis was inhibited by cytochalasin A or by iodoacetate; unlike iodoacetate, cytochalasin A did not cause accumulation of sugar phosphates. In contrast, cytochalasin A, but not iodoacetate, inhibited isolated membrane-bound ATPases. Cytochalasin A is a sulfhydryl-reactive agent and has membrane-related effects (adenosine triphosphatase) which may well be the basis of its interference with energy-dependent uptake of solutes.
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PMID:Action of cytochalasin A, a sulfhydryl-reactive agent, on sugar metabolism and membrane-bound adenosine triphosphatase of yeast. 12 88

The specificity of the histochemical localization of the calcium activated adenosine triphosphatase (ATPase) activity of the sarcoplasmic reticulum (SR) at pH 7.4 was studied using a calcium-citro-phosphate technique. The latter involves the splitting of ATP by ATPase producing phosphate ions which then react with calcium and citrate to form an insoluble reaction product. This reaction product was detected by both light and electron microscopy. Light microscopic examination showed a darkly stained continuous reticular pattern of reaction product which surrounded individual myofibrils. This reticular pattern of reaction product was distinctly dissimilar to that found when the histochemical reactions for mitochondrial or myofibrillar ATPase were performed. Ultrastructural investigations demonstrated the presence of discrete foci of electron dense reaction product in close association with the membranes of the SR in striated muscle fibres. Only occasional flecks were seen in the vicinity of mitochondria or myofilaments. The possibility is considered that the reticular pattern of staining achieved by the calcium-citro-phosphate technique may reflect the distribution of the "extra ATPase" of the SR, an enzyme implicated in the process of calcium uptake and muscle relaxation.
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PMID:On the specificity of the histochemical technique for sarcoplasmic reticular adenosine triphosphatase: a light and electron microscopic study. 12 15

Between birth and 10 days the mean growth rate of peroneus longus motor end plates was 0-298 mum/day. A similar rate was found in seven other muscles from different anatomical regions. At birth, sartorius spindles contained three types of intrafusal myofibres; (i) large diameter with conspicuously strong acid-stable, and moderate or strong alkali-stable adenosine triphosphatase (ATPase) reactions; (ii) large diameter with weak or negligible acid-stable and alkali-stable ATPase; (iii) small diameter with weak or negligible acid-stable, and strong alkali-stable ATPase. All had a high mitochondrial enzyme content and positive PAS reaction. With the exception of some large diameter fibres, all reacted positively for phosphorylase. The frequency distribution of diameters was unimodal at birth but by 9 or 10 days was bimodal.
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PMID:Growth of motor end plates and histochemistry of intrafusal myofibres in neonatal piglets. 12 8

Electron microscopic cytochemical localization of Mg++-activated adenosine triphosphatase (Mg++-ATPase) and 5-nucleotidase (AMPase) was investigated in bile canaliculus-rich and bile duct-containing fractions isolated from rat liver. Comparative cyochemical studies between prefixed and non-prefixed fractions revealed that the activity of both enzymes could be detected in the fractions under appropriate experimental conditions. However, the cytochemical activity of AMPase was much more sensitive to glutaraldehyde than that of Mg++-ATPase. Mg++-ATPase and AMPase reaction products were localized primarily on bile canalicular microvilli, that is, along the outer (luminal) surface of canalicular plasma membranes, but they were never observed on bile ductal microvilli. AMPase was also detectable on lateral hepatic plasma membranes. Mg++-ATPase demonstrated by the cytochemical technique described is a reliable enzyme marker for isolated bile canalicular membranes. At high magnification, Mg++-ATPase reaction product was also observed on the microfilaments surrounding isolated bile canaliculi. The possibility that the reaction product on the pericanalicular microfilaments may result from the hydrolysis of ATP byan actomyosin ATPase-like enzyme associated with these filaments is briefly discussed.
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PMID:Electron microscopic cytochemical characterization of bile canaliculi and bile ducts in vitro. 12 97

1. A procedure was developed for the preparation of plasma membranes from experimental granulation tissue of the rat without the addition of enzymes. The yield is better than 20% and the purification at least tenfold. 2. Values are given for the activities of 5'-nucleotidase, Na-+, k-+-activated Mg-2+dependent adenosine triphosphatase and leucine beta-naphthylamidase, for lipid composition, and for the gel-electrophoretic patterns of proteins and glycoporteins in the membrane preparations. 3. The plasma membranes from the mature granulation tissue contain proportionally more protein in the lipid phase, but the specific activities of 5'-nucleotidase and Na-+,K-+-activated Mg-2+-dependent adenosine triphosphatase are smaller than in the proliferating tissue. Certain differences were repeatedly observed in the gel-electrophoretic patterns of the developmental phases. 4. The plasma membranes from the granulation tissue were compared with those from rat peritoneal macrophages and from embryonic-chick tendon cells.
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PMID:Plasma membranes from experimental granulation tissue. 12 81

The dependence of the (Na-++K-+)-dependent ATPase (adenosine triphosphatase) (EC 3.6.1.3) on lipid has been examined in a number of different ways, with the use of various preparations from kidney tissue. The main findings were as follows. (1) The ATPase activities of the preparations examined were closely correlated with their total phospholipid content. (2) Extraction of the ATPase with deoxycholate or Lubrol W, combined with suitable salt-fractionation and washing procedures, removed phospholipid, cholesterol and enzymic activity in parallel; but activity was completely lost before all lipid had been removed. (3) The loss of activity could not be attributed to inhibition by residual detergent. (4) No selective removal of any particular phospholipid class by detergent could be detected. (5) Consistent reactivation of the Lubrol-extracted enzymes was obtained by adding dispersions of exogenous phospholipid, but only some, bearing a net negative charge, such as phosphatidylserine and phosphatidylglycerol, were effective. (6) The degree of reactivation was correlated with the amount of residual activity remaining after lipid depletion. (7) Partial purification of the ATPase, giving a 50-fold increase in specific activity, was not accompanied by selective enhancement of any particular class of phospholipid. We conclude that although the ATPase is dependent on phospholipid, only the reactivation results provide evidence for specificity.
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PMID:Lipid requirement of the membrane sodium-plus-potassium ion-dependent adenosine triphosphatase system. 12 82

The phosphorylation and dephosphorylation steps of the (Na-++K-+)-dependent ATPase (adenosine triphosphatase) (EC 3.6.1.3) reaction have been compared in 'normal', lipid-depleted and 'restored' membrane ATPase preparations. Partial lipid depletion was achieved by a single extraction with Lubrol W, and 'restoration' by adding pure phosphatidylserine. Gamma-32-P-labelled ATP was used for phosphorylation. The main findings were as follows. (1) Partial lipid depletion decreased but did not prevent Na-+-dependent phosphorylation, although it virtually abolished both Na-+-dependent and (Na-++K-+)-dependent ATPase activities. (2) 'Restoration' with phosphatidylserine produced an increment in phosphorylation that was the same in the presence and absence of added Na-+. (3) K-+ decreased the extent of Na-+-dependent phosphorylation of the depleted enzyme without producing a corresponding release of Pi. (4) K-+ rapidly decreased the extent of phosphorylation of the 'restored' enzyme to near-background value, with a concomitant release of Pi. (5) Na-+-dependent ATP hydrolysis was not restored. (6) The turnover of the 'restored' enzyme seemed to be higher than that of the 'normal' enzyme. The reaction sequence is discussed in relation to these results and the fact that the depleted enzyme retained about 50% of K-+-dependent phosphatase activity.
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PMID:Role of phospholipid in the intermediate steps of the sodium-plus-potassium ion-dependent adenosine triphosphatase reaction. 12 83

Dispersed cell cultures of guinea-pig epidermis have been maintained for up to 36 days. The progress of these cultures has been studied by phase contrast microscopy, the adenosine triphosphatase reaction, and cinephotomicrography. Langerhans cells have been identified and their behaviour studied, particularly in relation to keratinocytes.
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PMID:Langerhans cells in tissue cultures of guinea-pig epidermal cells. 12 92


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