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)

Evidence from various sources in the literature suggests that, in connection with DNA, ATP dephosphorylation can be used to provide energy for mechanical effects. Starting from this concept we have studied a novel DNA-dependent ATPase purified to 90% homogeneity from Escherichia coli. The enzyme has a peptide weight near 180 000 and, in high salt, is a monomeric, probably highly anisometric molecule. In salt-free buffer, where the ATPase activity is highest, the enzyme forms aggregates. ATP is the preferred substrate (Km 0.27 mM) and dephosphorylated at the gamma-position at a maximal rate near 10(4) molecules per enzyme monomer per min at 35 degrees C. A requirement for divalent cation is best satisfied by Mg2+ or Ca2+ and the requirement for DNA best by the single-stranded, circular DNA of phages phiX174 (Km 62 nM nucleotide) and fd indicating that the enzyme recognizes internal DNA regions. When saturated with E. coli DNA unwinding protein phiX DNA is not accepted but, once in contact with the DNA, the enzyme is little inhibited by unwinding protein. Apparently the unwinding protein interferes preferentially with the recognition of DNA. The enzyme does not detectably cleave DNA, and for this and genetic reasons is not identical with the recBC ATPase or the K12 restriction ATPase of the extracted cells. The enzyme is probably not identical either with the dnaB-product-associated ATPase or the ATPase activity found in DNA polymerase III holoenzyme under appropriate conditions, and it is certainly not identical with a DNA-dependent ATPase of molecular weight 69 000 from E. coli which has recently been purified. Attempts to ascribe the enzyme to other genes, including recA, lex and rep, have failed.
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PMID:Enzymic unwinding of DNA. 1. Purification and characterization of a DNA-dependent ATPase from Escherichia coli. 13 22

The relationship between bile salt-independent canalicular flow and ATPase activity in liver plasma membranes (LPM) enriched in bile canaliculi, was studied in control, hyperthyroid, and hypothyroid rats. Canalicular bile production was significantly increased in hyperthyroid rats (3.19 +/- 0.23 mul/min per g liver) compared to controls (2.27 +/- 0.24 mul/min per g liver), while it diminished in hypothyroid animals (1.58 +/- 0.17 mul/min per g liver). Although bile salt excretion was also increased in hyperthyroid animals (62.4 +/- 13.3 vs. 41.2 +/- 8.4 nmol/min per g liver), the stimulation in canalicular secretion was primarily related to enhancement of the bile salt-independent fraction of flow (2.47 mul/min per g liver in hyperthyroid rats vs. 1.67 mul/min per g liver in controls). LPM Na+, K+-ATPase activity doubled in hyperthyroid animals (21.5 +/- 5.8 vs. 10.7 +/- 3.1 mumol Pi/mg protein per h) while Mg++-ATPase activity remained unchanged and 5'-nucleotidase activity increased to a small but significant extent. In hypothyroid rats, bile salt excretion remained unchanged from control values so that the reduced secretion was entirely secondary to an inhibition of bile salt-independent secretion (1.19 mul/min per g liver). Na+, K+-ATPase activity in the LPMs from hypothyroid animals decreased by nearly 50% (5.4 +/- 1.6 mumol Pi/mg protein per h), although comparable reductions in the specific activity of Mg++-ATPase and 5'-nucleotidase were also observed. Administration of L-thyroxine to hypothyroid animals restored both bile salt-independent canalicular secretion and membrane enzymes to control values within 2 and 4 days, respectively. Sodium dodecyl sulfate gel electrophoresis demonstrated no significant changes in LPM protein fractions from any of the treatment groups. These studies indicate that thyroid hormone has a parallel effect on bile salt-independent canalicular secretion and LPM Na+, K+-ATPase activity, supporting the hypothesis that Na+ transport and Na+, K+-ATPase may be determinants of bile salt-independent canalicular flow.
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PMID:The effect of thyroid hormone on bile salt-independent bile flow and Na+, K+ -ATPase activity in liver plasma membranes enriched in bile canaliculi. 13 19

At [Na+]o = 118 mM the concentrative transfer of cholic and taurocholic acid from the perfusate into the isolated rat liver displays saturation kinetics (taurocholate: V = 299 nmol-min-1-g-1, Km = 61 muM; Cholate: V=327 nmol-min-1-g-1, Km = 436 muM). Perfusion with an isotonic sodium-free medium did not change the feature of a carrier-mediated transport but did markedly reduce V without affecting Km (taurocholate: V = 65 nmol-min-1-g-1, Km = 78 muM; cholate: V = 104 nmol-min-1-g-1, Km = 354 muM). It was experimentally assured that the observed reduction of bile salt uptake was not a consequence of regurgitation of bile salts or due to an excessive intracellular accumulation during cholestasis in the sodium-free state. The rate of taurocholate efflux is very low when compared with the rapid rate of the uptake. A stimulatory action of extracellular sodium on this pathway was also observed. Inhibition of the (Na+ + K+)-ATPase by 1 mM ouabain resulted in a decrease of bile salt uptake. Activation of the enzyme by potassium readmission to a K+-deprived liver enhanced bile salt uptake. The immediate response to alteration of the enzyme activity suggests a close association of a fraction of bile acid active transport with the sodium pump.
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PMID:Investigations on the sodium dependence of bile acid fluxes in the isolated perfused rat liver. 13 26

A new ATPase electrophoretically and immunologically distinct from the dynein ATPase studied previously has been solublized and purified from sea urchin sperm flagella. This ATPase has properties similar to those of dynein ATPase. Therefore, we propose that the two ATPases be considered as dynein isoenzymes, with previously studied dynein being known as dynein 1, and the newly discovered ATPase as dynein 2. Some physicochemical and enzymatic properties of dynein 2 have been determined. The molecular weight calculated from the sedimentation coefficient (12.3 "/- 1 S) and Stokes radius (12.8 "/- 0.4 nm) is 690,000 +/- 70,000. The molecular weight of the high molecular weight subunit of dynein 2 has been determined to be 325,000 +/- 40,000 by Na dodecyl-SO4-polyacrylamide gel electrophoresis. The enzymatic properties of dynein 1 and dynein 2 are similar in substrate specificity, pH optimum, and Mg2+ requirement for ATPase activity, but they differ in their Michaelis constant and in their dependence of ATPase activity upon salt concentration. Digestion of dynein 2 with trypsin yields an ATPase-containing protein fragment, similar to Fragment A obtained from dynein 1. An antiserum prepared against Fragment A from dynein 1 did not precipitate dynein 2 or inhibit its ATPase activity.
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PMID:Dynein 2. A new adenosine triphosphatase from sea urchin sperm flagella. 13 96

The purpose of this investigation was to determine whether or not the nasal glands of the roadrunner and the Coturnix quail show cytological specializations for salt secretion. In addition, the Na-K ATPase content of the quail gland was determined before and after drinking of saline solutions, in an effort to evaluate the functional status of the gland. The ability to maintain weight while drinking salt water was also measured as a general index of tolerance to saline conditions. The ultrastructure of the nasal glands of the roadrunner injected with salt and of quail drinking 200 mM NaCl was similar to that of salt glands in reptiles and the fresh-water acclimated duck. Numerous lateral cell evaginations and abundant mitochondria were present in the principal cell types. There was a significant increase in quail nasal gland Na-K ATPase when young birds were offered only saline solutions to drink. The ability of Coturnix quail to maintain weight while drinking saline solutions improves with age and at adulthood is comparable to that of some North American desert quail. Roadrunners were previously known to possess functional salt glands whereas quail were not. However the characteristic fine structure and the high Na-KATPase content of the quail nasal gland suggest that it is a salt gland.
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PMID:Evidence for the presence of nasal salt glands in the roadrunner and the Coturnix quail. 13 19

1. The presence of concanavalin A binding sugars in the glycoprotein component of a partially purified (Na++K+) ATPase preparation from dog fish salt gland was demonstrated by binding of a Triton X-100 extract of the enzyme and isolated glycoprotein to concanavalin A-Sepharose, and by binding of membrane-associated enzyme to free concanavalin A. 2. The binding of concanavalin A to the glycoprotein in both membrane-associated enzyme and a Lubrol extract of the enzyme had no effect on (Na++K+)-ATPase activity. Binding was completely inhibited by methyl-alpha-mannoside. Also, enzyme activity was not affected by removal of 50% of glycoprotein sialic acid by neuraminidase. These results suggest that the carbohydrate moiety of the glycoprotein does not play a catalytic role in the (Na++K+)-ATPase. 3. When a Triton X-100 extract of (Na++K+)-ATPase was chromatographed on concanavalin A-Sepharose, 37% of total protein was bound to the column and eluted by methyl-alpha-mannoside. The bound fraction was free of lipid, and contained not only the glycoprotein but also the large protein which is the catalytic subunit of the enzyme, and small amounts of other membrane derived proteins. The ratio of large protein to glycoprotein, as measured by the relative Coomassie blue absorbance of the two proteins separated by gel electrophoresis, was the same in the bound fraction as in the membrane. These results suggest that the glycoprotein and lareg protein are either associated together in the membrane or become associated during lipid replacement by Triton.
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PMID:Studies on the glycoprotein component of (Na+ +K+)-ATPase from dog fish salt gland. Binding to concanavalin A and removal of sialic acid by neuraminidase. 13 94

Hypertensive Goldblatt-rats have higher than normal Na-appetite and an enhanced Na-output. They have normal plasma Na- and K-concentration and kidney weight but a significantly reduced plasma volume. The amount of renal membrane protein and the renal Na-K-ATPase-activity of hypertensive rats was found to be significantly below that of controls. In order to evaluate the role of Na-appetite, Na-excretion rate and renal Na-K-ATPase-activity in the electrolyte balance, Goldblatt-rats with a stable hypertension and control animals were put for 8 days on a Na-free diet. Na-excretion rate of control rats reached a minimum (13 muEq/100 g x 24 hr) within 5 days and was maintained on this level up to the end of the experiment. Na-free diet did not alter either the kidney weight or the amount of membrane protein of the animals. However, in salt-free fed control rats total renal Na-K-ATPase-activity was found elevated by about 10% as compared to animals maintained on normal diet. Goldblatt-rats continuously excreted significantly higher amounts of Na (35 muEq/100 g x 24 hr), had sharply reduced plasma volume and plasma Na- concentration. The renal Na-K-ATPase-activity should no adaptation in gold blatt-rats. In all animals studied the rate of Na-excretion showed a close indirect correlation with the renal Na-K-ATPase-activity. It is concluded, that Goldblatt-rats depend on dietary Na to a higher extent than controls because of their reduced capacity to retain Na. The increased Na-appetite of hypertensive rats is a factor secondary to Na-loss.
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PMID:Interdependence of Na-excretion, plasma electrolytes, plasma volume and renal Na-K-ATPase-activity in hypertensive rats. 13 99

The soleus muscle of adult chicken was studied histochemically. Succinic dehydrogenase (SDH) and myofibrillar ATPase reactions, with or without preincubation in K2-EDTA salt, were compared in serial frozen sections. Based upon the distributions of the above reactions, the three major fibre types distinguished were "Type I red", "Type II red" and "Type II white". On the basis of non preincubated ATPase reaction alone two sub-types of type I red fibres could be distinguished. However, following preincubation in a "Cold" solution of K2-EDTA, Type II red fibres fell into two sub-types and Type II white fibres fell into three sub-types. Amalgamating the two already existing classifications, a more elaborate classification is presented for characterizing these different sub-types. The presence of two different or a spectrum of staining variations in a seemingly homogeneous population of muscle fibres in a given fibre-type emphasizes the possible correlation between this histochemical data and the heterogeneity of contraction times of the different motor units.
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PMID:Histochemical sub-types of three fibre-types of avian skeletal muscle. 13 25

Membranes were purified from rat muscle by a differential centrifugation method that avoids the use of salt extraction or incubations at elevated temperature. Three populations of membrane-limited vesicles were defined having average densities of 1.112 (fraction I), 1.141 (fraction II), and 1.158 (fraction III) g/ml in a continuous sucrose gradient. Lactoperoxidase-catalyzed iodination of intact muscle prior to isolation of membranes resulted in highest specific activity in fraction I, although all fractions could be equally labeled after isolation. 125I-Labeled wheat germ agglutinin incubated at low concentration with intact muscle preferentially labeled fraction I. Parallel studies on previously isolated fractions indicated that fraction I also contained the highest concentration of potential receptors for wheat germ agglutinin. In experiments on whole muscle, concanavalin A bound predominantly to sarcolemma with slight variable binding to T-tubular and nuclear membrane but no binding to sarcoplasmic reticulum or mitochondria. Parallel binding studies with isolated membrane fragments indicated heavy binding of concanavalin A by membranes in fraction I with scattered binding in fractions II and III. Na+K+Mg2+ ATPase was specifically enriched in fraction I but was also present in fraction II in a proportion similar to 125I labeling. Ca2+ ATPase was most active in fraction II but present in significant levels in fraction I. It is concluded from these and other data that fraction I contains predominantly sarcolemma membrane, while T-tubular membrane may represent a significant component of fraction II. Ca2+ ATPase activity in fraction I is intrinsic to the sarcolemma.
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PMID:Isolation and characterization of muscle membranes using surface-specific labels. 13 40

Juvenile rats fed a diet containing 1% lead acetate for 7 weeks, in addition to an impaired growth rate and renal function derangements, suffered malabsorption of glucose and certain amino acids, as assessed by an in vivo perfusion technique. The reduction in glucose absorption ranged between 10% and 31% when the carbohydrate was pumped in concentrations of 2-80 mM. This alteration was compatible with a noncompetitive type of transport inhibition. The intestinal absorption of glycine, lysine, and phenylalanine were, respectively, decreased 22, 18, and 15% when these amino acids were present at 1 mM levels. Sodium transport was severely reduced (57.6 +/- 17.9 (SEM) vs. 124.2 +/- 17.4 muEq/min-cm) and intestinal mucosa (Na+-K+)-ATPase was concomitantly lower in the lead-intoxicated rats (186.4 +/- 19.0 vs 268.4 +/- 29.8 nmol P/min-mg protein). However, this enzyme was not altered in liver and kidney. Furthermore, intestinal mucosa fructose-1,6-diphosphatase, succinic dehydrogenase, pyruvate kinase, and tryptophan hydroxylase were not different in experimental and control animals. These studies substantiate the presence of functional and biochemical abnormalities in the intestinal mucosa of young rats when fed substantial amounts of a soluble lead salt. It is, therefore, reasonable to accept the possibility that physiologic damage occurs in tissues directly subjected to high and persistent levels of a toxic agents, as it occurs in other organs, underscoring the parallelism between transport mechanisms at the renal and intestinal levels.
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PMID:Experimental lead poisoning and intestinal transport of glucose, amino acids, and sodium. 13 38


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