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)

Normal and diseased human muscle cells have been grown in combined cultures with 12-14 day embryonic mouse spinal cord explants. Nerve endings on myotubes were found by light and scanning electron microscopy, and motor end-plates were identified by a histochemical reaction for acetylcholinesterase. Contracting myotubes, never observed in cultures of human muscle alone, were found in a culture from normal muscle. Histochemical studies demonstrated the presence of strongly and weakly reacting myotubes for both ATPase pH 9.4 and NADH-TR, but could not be related to the development of fibre types. No differences in morphology or histochemical reactions were found between normal and diseased muscle cells in these combined cultures.
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PMID:Growth of diseased human muscle in combined cultures with normal mouse embryonic spinal cord. 12 4

By crossed immunoelectrophoresis with membrane antiserum, 17 antigens have been detected in fractions from plasma membranes of M. lysodeikticus solubilized with Triton X-100. Absorption tests with protoplasts have demonstrated that eight of the antigens are expressed on the surface. Of these antigens the major one has been identified as a succinylated mannan. Five of the principal immunoprecipitates unaffected by absorption with protoplasts were shown by zymograms to possess the following enzymic activites: succinate dehydrogenase (EC 1.3.99.1), ATPase (EC 3.6.1.3), NADH dehyrogenase (EC 1.6.99.3)(two separate components), and malate dehydrogenase (EC 1.1.1.37). These enzymes or enzyme-complexes are, therefore, not expressed on the outer surface of the protoplast membrane.
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PMID:Antigenic and enzymatic architecture of Micrococcus lysodeikticus membranes established by crossed immunoelectrophoresis. 12 77

Muscle samples were obtained from the gastrocnemius of 17 female and 23 male track athletes, 10 untrained women, and 11 untrained men. Portions of the specimen were analyzed for total phosphorylase, lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) activities. Sections of the muscle were stained for myosin adenosine triphosphatase, NADH2 tetrazolium reductase, and alpha-glycerophosphate dehydrogenase. Maximal oxygen uptake (VO2max) was measured on a treadmill for 23 of the volunteers (6 female athletes, 11 male athletes, 10 untrained women, and 6 untrained men). These measurements confirm earlier reports which suggest that the athlete's preference for strength, speed, and/or endurance events is in part a matter of genetic endowment. Aside from differences in fiber composition and enzymes among middle-distance runners, the only distinction between the sexes was the larger fiber areas of the male athletes. SDH activity was found to correlate 0.79 with VO2max, while muscle LDH appeared to be a function of muscle fiber composition. While sprint- and endurance-trained athletes are characterized by distinct fiber compositions and enzyme activities, participants in strength events (e.g., shot-put) have relatively low muscle enzyme activities and a variety of fiber compositions.
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PMID:Skeletal muscle enzymes and fiber composition in male and female track athletes. 12 49

Exposure of rat brain Na+ + K+-ATPase (ATP phosphohydrolase E.C. 3.6.1.3) to concentrations of cassaine greater than 1 x 10(-4) M resulted in a poorly reversible inhibition of this enzyme. Inhibition did not require the presence of ATP and developed rapidly, but the final amount of inhibition observed was independent of time. The amount of inhibition observed at a given concentration of cassaine was reduced by increasing the concentration of membranes in the system. The inhibition of Na+ + K+-ATPase activity was associated with equivalent inhibition of the phosphorylation and (3H)-ouabain binding reactions of this enzyme, while the uninhibited enzyme was apparently kinetically normal. Concentrations of cassaine which produced this stable inhibition of Na+ + K+-ATPase had no effect on the Mg2+-activated ATPase or the NADH cytochrome-c-reductase activities of crude rat brain microsomal preparations. Cassaine inhibited the cholinesterase activity of rat brain microsomes with a Ki of about 5 x 10(-5) M, but his inhibition was fully reversible. The poorly reversible inhibitory actions of cassaine, thus, appeared specific for Na+ + K+-ATPase. Because this stable pattern of inhibition of the Na+ + K+-ATPase by cassaine required drug concentrations at least one hundred-fold greater than those which produce positive inotropic effects, it appears unlikely that this pattern of Na+ + K+-ATPase inhibition is involved in the cardiotonic actions of this drug.
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PMID:Studies on the stable inhibition of Na+ + K+-ATPase by cassaine. 13 Feb 44

Frozen sections of equine musculus semitendinosus were examined for myosin adenosine triphosphatase (ATPase) and reduced nicotinamide adenine dinucleotide-tetrazolium reductase (NADH-TR), using standard histochemical procedures, and the proportions of the various fiber types and average fiber sectional size were determined. With ATPase staining, approximately 70% of the fibers were classified as alpha fibers (ATPase positive), and 30%, as beta fibers (ATPase negative). In addition, 2 populations of alpha fibers could be readily distinguished on the basis of the intensity of the ATPase reaction, and these were designated alpha positive and alpha intermediate. The relationship of this difference in ATPase reaction to contraction speed of the fibers is not known. With NADH-TR staining, fibers were classified as either red fibers (positive) having aerobic metabolism or white fibers (negative) having primarily anaerobic metabolism. All beta fibers were red by NADH-TR; thus, they conformed to the criteria for beta R fibers. All alpha positive fibers were white by NADH-TR, as were most of the alpha intermediate fibers, and would be classified alpha W. Some of the alpha intermediate fibers gave an intermediate reaction with NADH-TR and could be classified as alpha R fibers which have not transformed to alpha W fibers. The alpha positive fibers were 7 to 10 mum larger in diameter than either beta or alpha intermediate fibers.
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PMID:Fiber types and size in equine skeletal muscle. 13 Aug 14

1. Oxidative phosphorylation was reconstituted with a mitochondrial proton pump (oligomycin-sensitive ATPase) and segments of the oxidation chain (cytochrome oxidase or DPNH-Q1 reductase). A proton pump of bacteriorhodopsin substituted for the respiratory chain components, giving rise to light-induced ATP formation. 2. Since oxidative phosphorylation has thus become a special case of the problem of ion translocation in general, we have investigated and reconsituted other pumps. The reconstituted Ca++ pump of sarcoplasmic reticulum consists of two factors, the Ca++-dependent ATPase and a heat-stable coupling factor. 3. Other information obtained from reconstitution experiments include the role of asymmetry in organized membranes and the specificity of protein-phospholipid interaction. 4. Purified preparations of Ca++-ATPase catalyze the formation of ATP from Pi and ADP in a stepwise reaction stoichiometric with the enzyme and dependent on Ca++.
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PMID:Resolution and reconstitution of ion-transport systems. 13 Aug 18

Measurement of certain membrane-bound enzymic activities was used to study the orientation of the outer membrane of the double-membraned forespore of Bacillus megaterium KM. 2. Adenosine triphosphatase, NADH dehydrogenase and L-malate intact protoplasts, but were readily detected in intact stage II or IV forespores, consistent with reversed polarity of the outer forespore membrane relative to the mother-cell plasma membrane. 3. Measurement of NADH oxidase activity revealed that intact stage III forespores had the same high affinity for NADH as protoplast membrane preparations and protoplast lystates, consistent with ready access of NADH to oxidation sites on the outer forespores membrane. 4. Forespores and protoplasts showed osmometric behaviour in solutions of non-permanent solutes consistent with the presence of an intact permeability barrier in these structures.
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PMID:Biochemical evidence for the reversed polarity of the outer membrane of the bacterial forespore. 13 69

Membrane vesicles were prepared by osmotic lysis of spheroplasts from M13-infected Escherichia coli. Reduced nicotinamide adenine dinucleotide (NADH) oxidase (reduced NAD: oxidoreductase, EC 1.6.99.3) and Mg2+-Ca2+-activated adenosine triphosphatase (ATP phosphohydrolase, EC 3.6.1.3), which are normally localized to the inner surface of the cytoplasmic membrane, were 50% acceesible to their polar substrates in these vesicles. The major coat protein of coliphage M13 is also bound to the cytoplasmic membrane (prior to phage assembly) but with its antigenic sites exposed to the exterior of the cell. Antibody to M13 coat protein was used to fractionate membrane vesicles. Neither agglutinated nor unagglutinated vesicles had altered NADH oxidase and adenosine triphosphatase specific activities. This is inconsistent with such vesicles being a mixture of correctly oriented and completely inverted membrane sacs and suggests that NADH oxidase, adenosine triphosphatase, M13 coat protein, or all three proteins rearrange during vesicle preparation.
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PMID:Fractionation of membrane vesicles from coliphage M13-infected Escherichia coli. 13 27

The ATPase reaction and its pH lability demonstrate three fiber types in the adult mouse gastrocnemius; Type I (light staining with alkaline preincubation and dark with acid preincubation), Type IIA (dark after alkaline preincubation), type IIB (dark after alkaline and acid preincubation). The SDH and NADH-tetrazolium reductase reactions also demonstrate three types of fibers; those low (A), intermediate (B) or high (C) in oxidative enzyme activity. However, the use of both procedures in serial sections demonstrates that four different combinations occur; the IIB fibers are high in SDH activity, the I fibers are intermediate in SDH enzyme activity, while the IIA fibers are either low or intermediate in SDH activity. These fiber types are present within the gastrocnemius muscle in a distinct pattern of zones. The predominant fiber type, located in the superficial half of the muscle, is the IIA (A) fiber which is high in ATPase and low in SDH activity. This is consistent with the fact that the gastrocnemius is generally considered a white, fast muscle. The IIB and I fibers are fewer in number and are located deeper in the muscle.
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PMID:Skeletal muscle fiber types in the adult mouse. 13 38

Four cytoplasmic mutants of Saccharomyces cerevisiae showing loss of mitochondrial rutamycin-sensitive ATPase activity but having significant cytochrome oxidase and NADH-cytochrome c reductase have been isolated. Genetic studies indicate the mutations to be closely linked to each other and have been assigned to a new locus, PHO1. The mutations show a low frequency of recombination with the OL12 locus, suggesting a linkage to this marker. They are not, however, linked to the OLI1 locus. Linkage of the ATPase mutations to the OLI2 locus is also indicated by restoration of wild-type diploids by sigma- clones that retain the segment of mitochondrial DNA carrying OLI2. Based on the recombinants issued from crosses of the mutants with a triple drug-resistant strain and an analysis of the resistance markers present in sigma- clones that are effective in restoring a wild-type phenotype, the PHO1 locus has been placed in the segment of DNA located between PAR1 and OLI2.
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PMID:Localization on mitochondrial DNA of mutations leading to a loss of rutamycin-sensitive adenosine triphosphatase. 13 92


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