Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Embryonal rhabdomyosarcomas from the nasopharynx of two children were examined by histochemical methods commonly applied to muscle biopsies. These stains included nicotinamide adenine dinucleotide-tetrazolium reductase (NADH-TR), succinate dehydrogenase (SDH), PAS, PAS-diastase, myophosphorylase, calcium-mediated adenosine triphosphatase (ATPase) preincubated at high and low pH, and oil red O. Myofibrils were easily identified with ATPase and blood vessel walls were also stained. NADH-TR clearly showed longitudinal and cross-striations that were not seen with H&E or PTAH stains. The modified Gomori trichrome stain additionally contributed to the recognition of myofibrils. Some techniques of muscle histochemistry applied to fresh frozen sections of tumor tissue may provide evidence of muscular differentiation in otherwise poorly differentiated sarcomas for a more accurate diagnosis of rhabdomyosarcoma.
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PMID:Diagnostic value of histochemistry in embryonal rhabdomyosarcoma. 9 52

In the gastrocnemius muscle of cat and rat, staining for oxidative enzymes differentiated three fiber types (A,B,C) and staining for adenosine triphosphate at pH 9.4 differentiated two fiber types (I, II) with a reliability of 90% and 98%, respectively. In cat 96% and in rat 90% of the fibers were typed identically after staining for nicotinamide adenine dinucleotidelinked lactic dehydrogenase (LDH) and succinic dehydrogenase (SDH). When differentiated by staining for LDH, A and B fibers were of type I. IN RAT, 80-90% OF ALL FIBERS WERE OF TYPE 22, COMPPRISING A, B and C fibers. Type I fibers stained for LDH intensely as did C fibers of type II, but stained intermediately for SDH. The degree of staining was measured by photometry. When fibers were stained for LDH, histograms of density showed three peaks corresponding to A, B and C fibers in cat, but only two peaks corresponding to A and C fibers in rat, In cat and rat, the densities of A, B and C fibers belonged to different populations. In soleus muscle of cat and rat stained for LDH, menadione-linked alpha-glycerophosphate dehydrogenase and adenosine triphosphatase at pH 9.4, the degree of staining differed from thatin any type of fiber in gastrocnemius muscle
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PMID:Histochemical fiber typing and staining intensity in cat and rat muscles. 12 97

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

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

Membranes were isolated and purified from nutrient broth-yeast extract- and hexadecane-grown cells of Acinetobacter sp. strain HO1-N. Two membrane fractions were isolated from nutrient broth-yeast extract-grown cells, the cytoplasmic membrane and the outer membrane. In addition to these two membrane fractions, a unique membrane fraction was isolated from hexadecane-grown cells (band 1) and characterized as a lipid-rich, low-density membrane containing high concentrations of hexadecane. The outer membrane preparations of Acinetobacter, obtained from nutrient broth-yeast extract- and hexadecane-grown cells, exhibited a low ratio of lipid phosphorus to protein and contained phospholipase activity and 2-keto-3-deoxyoctulosonic acid. Phosphatidic acid cytidyltransferase, adenosine triphosphatase, and reduced nicotinamide adenine dinucleotide oxidase were recovered almost exclusively in the cytoplasmic membrane fractions. The cytoplasmic membrane fractions contained 20 to 25 polypeptide species on sodium dodecyl sulfate-polyacrylamide gels, and the outer membrane fractions contained 15 to 20 polypeptide species. A major polypeptide species with an apparent molecular weight of approximately 42,000 to 44,000 was found for all outer membrane fractions. The buoyant densities of the cytoplasmic membrane fractions and the outer membrane fractions were closely similar, necessitating their separation by differential centrifugation. Band 1 of hexadecane-grown cells had a ratio of lipid phosphorus to protein that was almost twice that of cytoplasmic membrane and a correspondingly low buoyant density (1.086 g/cm3). Enzyme activities associated with band 1 were identical to those associated with the cytoplasmic membrane. The electrophoretic banding pattern of band 1 was essentially identical to the banding pattern of the cytoplasmic membrane. The phospholipid and neutral lipid compositions of the isolated membrane fractions were determined as qualitatively similar, with significant quantitative differences. The ultrastructure characteristics of the respective membrane fractions were examined by the negative-stain technique.
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PMID:Isolation and characterization of membranes from a hydrocarbon-oxidizing Acinetobacter sp. 13 29

The histochemical profiles of myofibrillar adenosine triphosphatase (ATPase), nicotinamide adenine dinucleotide diaphorase (NADDase), and phosphorylase (Pase) activities were studied in the respiratory muscles of the chicken. Most respiratory muscles contained fibers exhibiting 18 possible combinations of staining reactions (dark or light ATPase; dark, intermediate, or light NADDase; dark, intermediate, or light Pase). Fibers that stained light for ATPase constituted as little as 10% of the total population in rectus abdominis, but as much as 32% of the total in costosternalis pars major. Those fibers did not tend to be smaller than fibers that stained dark for ATPase in the respiratory muscles as a group. Assuming these staining characteristics are correlated with functional properties of the fibers, as they are in mammals, the majority of the fibers should contract rapidly (dark ATPase) and be fatigue resistant (dark and intermediate NADDase).
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PMID:Histochemical studies of respiratory muscles of chicken. 14 96

Premature infants tolerate respiratory loads poorly. This may reflect incomplete development of the ventilatory muscles (VM) causing poor resistance to fatigue. To study the developmental pattern of human VM, 31 postmortem specimens of diaphragm and intercostal muscles were obtained. Individual muscle fibers were classified as type I (slow-twitch, high-oxidative) or type II (fast-twich, low-oxidative) using histochemical staining methods for myofibrillar adenosine triphosphatase (M-ATPase) (pH 10.30) and nicotinamide adenine dinucleotide (NADH) tetrazolium reductase. In the diaphragm, premature infants (less than 37 wk gestation) had only 9.7 +/- 1.3% type I fibers, full-term newborns 25.0 +/- 1.1%, and older subjects (greater than 2 yr of age) 54.9 +/- 1.3%. There was no further increase after 8 mo postpartum. In the intercostal muscles, premature infants had only 19.0 +/- 4.8% type I fibers, full-term newborns 45.7 +/- 1.3%, and older subjects 65.2 +/- 2.6%. There was no further increase after 2 mo postpartum. These findings suggest the ventilatory muscles of newborn infants are more susceptible to fatigue than those of older subjects. This may contribute significantly to respiratory problems in the neonate.
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PMID:Developmental pattern of muscle fiber types in human ventilatory muscles. 14 79

Mean fiber diameters and percentages of each fiber type of the vastus lateralis, vastus medialis, rectus femoris, and vastus intermedius muscles from 15 sheep, ranging from 1 day to 5 years of age, were determined. Myosin adenosine triphosphatase and nicotinamide adenine dinucleotide-tetrazolium reductase stained sections were used. The vastus lateralis, vastus medialis, and rectus femoris contained 3 fiber types (I, IIA, and IIB). The vastus intermedius was composed almost entirely of type I fibers. From birth to 5 years of age, mean fiber diameters of type I fibers increased from 15.8 to 47.0 micron in the vastus lateralis, 15.6 to 50.7 micron in the vastus medialis, 17.5 to 46.5 micron in the rectus femoris, and 26.7 to 51.8 micron in the vastus intermedius. Means of fiber diameters of type II fibers increased from 16.1 to 44.6 micron in the vastus lateralis, 19.8 to 44.0 micron in the vastus medialis, and 17.0 to 44.5 micron in the rectus femoris. The percentage of type II fibers in the vastus lateralis, vastus medialis, and rectus femoris decreased from 85% to 90% at birth to approximately 72% at 5 years of age. The vastus intermedius consisted of only type I fibers in sheep 2 years and older.
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PMID:Age-related changes in percentage of fiber types and mean fiber diameters of the ovine quadriceps muscles. 15 22

Cytochrome-deficient cells of a strain of Escherichia coli lacking 5-amino-levulinate synthetase have been used to study proton translocation associated with the reduced nicotinamide adenine dinucleotide (NADH) dehydrogenase region of the electron transport chain. Menadione was used as electron acceptor, and mannitol was used as the substrate for the generation of intracellular NADH. The effects of iron deficiency on NADH- and D-lactate-menadione reductase activities were studied in iron-deficient cells of a mutant strain unable to synthesize the iron chelator enterochelin; both activities were reduced. The NADH- menadione reductase activity in cytochrome-deficient cells was associated with proton translocation and could be coupled to the uptake of proline. However proton translocation associated with the NADH-menadione reductase activity was prevented by a mutation in an unc gene. It was concluded that there is no proton translocation associated with the NADH-dehydrogenase region of the electron transport chain in E. coli and that the proton translocation obtained with mannitol as substrate is due to the activity of membrane-bound adenosine triphosphatase.
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PMID:Proton translocation in cytochrome-deficient mutants of Escherichia coli. 15 8

The antigenic composition and molecular structure of the plasma membrane of Streptococcus pyogenes (group A; M type 6) were studied by crossed immunoelectrophoresis (XIE) and other related quantitative immunoelectrophoretic techniques. After establishment of a reference pattern of 29 immunoprecipitates, the relative differences in amounts of individual antigens contained in membranes isolated from cells that were harvested during the exponential or stationary phase of growth were examined. Relative increases and decreases in amounts of individual antigens were estimated from the areas subtended by immunoprecipitates after XIE of Triton X-100 extracts. The asymmetric distribution of antigens on the inner and outer surfaces of the membrane was established in absorption experiments with intact, stable protoplasts. Of the 29 immunoprecipitates, 8 appeared to contain antigens exposed on the outer surface of the membrane, whereas 11 appeared to contain antigens either located on the inner surface or unexposed. Six antigens appeared to have limited exposure on the outer surface, and four others remain to be assigned. Certain immunoprecipitates were characterized with respect to enzymatic activity or interaction with the lectin concanavalin A. Reduced nicotinamide adenine dinucleotide dehydrogenase (EC 1.6.99.3), adenosine triphosphatase (EC 3.6.1.3), and polynucleotide phosphorylase (EC 2.3.7.8) were demonstrated by zymogram techniques. The latter two activities were present within the same immunoprecipitate, suggesting the occurrence of a multienzyme complex. In addition, the areas under the immunoprecipitates containing the three enzymatic activities were not affected by absorption of antimembrane immunoglobulin with intact protoplasts and thus appeared to be located on the inner surface of the membrane. The results from absorption experiments also suggested that the exposure of outer protoplast surface antigens was greater on protoplasts from exponential-phase cells than on those from stationary-phase cells, even when found in increased amounts in the latter.
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PMID:Quantitative immunoelectrophoretic analysis of Streptococcus pyogenes membrane. 16 Aug 91


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