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)

For determination of 3 muscle fiber types in equine skeletal muscle, a comparison of 2 preincubation buffers, each followed by myosin adenosine triphosphatase staining, was made. Serial sections of the muscle samples (n = 75) were preincubated in an acid buffer (pH 4.6) or a formaldehyde-glycine buffer (pH 7.25) and then were stained for myosin adenosine triphosphatase. Differentiation of muscle fibers into type I, IIA, and IIB was identical with both techniques; however, in the samples prepared at pH 4.6, type I fibers were black; type IIA, light gray; and type IIB, dark gray. In the samples prepared at pH 7.25, types I, IIA, and IIB fibers were white, light gray, and dark gray respectively. The formaldehyde-glycine preincubation buffer (at pH 7.25) gave more consistent results, was easier to prepare, and retained cytoarchitecture better, compared with the samples prepared at pH 4.6.
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PMID:Simplified technique for histochemical determination of three fiber types in equine skeletal muscle. 619 24

A procedure is described which simplifies the classification of skeletal muscle fibres in that it allows a simultaneous evaluation of both the oxidative capacity and the intensity of "reversed" ATPase of the fibres, and thus enables to distinguish three fibre types - SO, FOG and FG - in one tissue section. After preincubation at pH 4.1-4.2 the cryostat section is incubated for succinate dehydrogenase (SDH) and subsequently for "reversed"-ATPase. This is followed by the fixation with neutral buffered formaldehyde. The results of typing of chicken, minipig and rabbit fibres in a single muscle section stained with this technique are identical to those obtained with the usual method based on a comparison of serial sections of which one is stained for SDH activity the other for "reversed"-ATPase activity.
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PMID:A successive histochemical staining for succinate dehydrogenase and "reversed"-ATPase in a single section for the skeletal muscle fibre typing. 622 54

Simian virus 40 (SV40)-transformed monolayer cells were analyzed in situ by indirect immunofluorescence microscopy for the postulated cell surface location of SV40 T-antigen-related molecules. With antisera prepared against purified, sodium dodecyl sulfate-denatured SV40 T-antigen, positive surface staining was obtained when the cells had been treated with formaldehyde before immunofluorescence analysis. In contrast, living SV40-transformed cells analyzed in monolayer were surface fluorescence negative. The fixation procedure developed in this study combined with a double staining immunofluorescence technique allowed the simultaneous analysis of the same cells for the expression of both SV40 T-antigen-related surface antigen and nuclear T-antigen. The localization of SV40 T-antigen-related surface antigen on the outer surface of the plasma membrane of formaldehyde-fixed SV40-transformed cells was demonstrated directly by the protein A-mediated binding of Staphylococcus aureus bacteria on formaldehyde-fixed SV40-transformed cells precoated with antiserum against sodium dodecyl sulfate-denatured T-antigen. Both cell surface staining and S. aureus binding were found to be highly specific for SV40 T-antigen-related binding sites. These results indicate that T-antigen-related molecules in a cryptic form are located on the surface of SV40-transformed monolayer cells and can be detected in situ after modification of the cell surface architecture.
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PMID:Simian virus 40 T-antigen-related cell surface antigen: serological demonstration on simian virus 40-transformed monolayer cells in situ. 625 89

The effects of mild periodate exposure on the kinetics of (Na+ + K+)-ATPase and K+-p-nitrophenylphosphatase were studied using rat cerebral microsome preparations. Fifty percent inhibition of both enzyme activities was attained near 3 microM periodate concentrations. This inhibition was biphasic with time. Mg2+-ATPase and Mg2+-p-nitrophenylphosphatase activities were much less inhibited by periodate. Periodate inhibition was partially reversed by dimercaprol and dithiothreitol but not by diffusion. The possible reaction products formic acid, formaldehyde, glyceraldehyde, and acetaldehyde had no inhibitory effects in similar concentrations. Periodate exposure produced no detectable changes in the activation of (Na+ + K+)-ATPase by Na+, K+, Mg2+, or ATP. Residues shared by both (Na+ + K+)-ATPase and K+-p-nitrophenylphosphatase are both critical to hydrolytic function and sensitive to mild oxidation by periodate.
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PMID:Inhibition of rat brain microsomal (Na+ + K+)-ATPase and K+-p-nitrophenylphosphatase by periodic acid. 628 25

Compound 48/80, a condensation product of N-methyl-p-methoxyphenethylamine with formaldehyde, is composed of a family of cationic amphiphiles differing in the degree of polymerization. Compound 48/80 was found to be a potent inhibitor of the calmodulin-activated fraction of brain phosphodiesterase and red blood cell Ca2+-transport ATPase, with IC50 values of 0.3 and 0.85 micrograms/ml, respectively. However, the basal activity of both enzymes is not at all suppressed by the drug at concentrations up to 300 micrograms/ml. Inhibition of Ca2+ transport into inside-out red blood cell vesicles by compound 48/80 follows a similar pattern in that basal, calmodulin-independent, transport is also not affected by the drug. Kinetic analysis revealed that the stimulation of Ca2+-transport ATPase induced by calmodulin is inhibited by compound 48/80 according to a competitive mechanism. It was demonstrated that the inhibitory constituents of compound 48/80 bind to calmodulin in a Ca2+-dependent fashion. Comparison of the specificity of several anti-calmodulin drugs showed that compound 48/80 is the most specific inhibitor of the calmodulin-dependent fraction of red blood cell Ca2+-transport ATPase that has been described hitherto. In addition, compound 48/80 was found to be a rather specific inhibitor of the calmodulin-induced activation of Ca2+-transport ATPase when compared with the stimulation induced by an anionic amphiphile or by limited proteolysis. Half-maximal inhibition of the activity stimulated by oleic acid or mild tryptic digestion required 8- and 32-times higher concentrations of compound 48/80, respectively, compared with the calmodulin-dependent fraction of the ATPase activity. Moreover, calmodulin-independent systems as rabbit skeletal muscle sarcoplasmic reticulum Ca2+-transport ATPase or calf cardiac sarcolemma (Na+ + K+)-transport ATPase are far less influenced by compound 48/80 as compared with trifluoperazine and calmidazolium. Because of its high specificity compound 48/80 is proposed to be a promising tool for studying calmodulin-dependent processes.
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PMID:Compound 48/80 is a selective and powerful inhibitor of calmodulin-regulated functions. 631 27

The distribution of ATPase activity in the flight muscle of Locusta migratoria L. was studied at the fine structural level after a brief fixation in formaldehyde or in glutaraldehyde. In both the cases, the final product of reaction -- fine grained electron dense precipitation--was clearly revealed in intact contractile muscle structures. The glutaraldehyde fixation provides a good preservation of all the ultrastructural components of muscle cell, and reveals deposites of the final product in sarcomeres at the resting length. However, after the glutaraldehyde fixation it is very difficult to recognize regions of fibrillar reaction on electronmicroscopic preparation. The formaldehyde fixation does not provide a good preservation of membranous structures. However after the formaldehyde fixation reacting regions are more extensive than after glutaraldehyde fixation, and, moreover, it is possible to demonstrate a correlation between the activity and the contraction of sarcomere.
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PMID:[Electron microscopic detection of ATPase activity in insect muscle after fixation with different fixatives]. 644 79

Pekin and Muscovy breeds of domestic ducks were reared from hatching to 10 weeks. Males and females of each breed were killed at weekly intervals and sartorius muscles were removed after the onset of rigor mortis. Fiber diameters were measured from macerated preparations after fixation with formaldehyde. All volumetric data were corrected to a common sarcomere length. Longitudinal and radial growth of muscles reached their maximum velocity during the fourth and fifth weeks, respectively. In Muscovies, heavier muscles in males relative to females were due to increased muscle length and cross sectional area. Faster early growth of Pekins relative to Muscovies was due to muscle length and fiber diameter. Histochemical analysis of supracoracoideus muscles frozen immediately postmortem showed that both adenosine triphosphatase and succinate dehydrogenase activity were negatively correlated with muscle fiber cross sectional area.
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PMID:Volumetric growth of muscle fibers in ducks. 645 44

Formalin-fixed myosin adenosine triphosphatase preparations of Syrian hamster quadriceps muscle showed myofibers distributed as follows: (1) vastus intermedius--light and dark fibers; (2) vastus medialis, rectus femoris, and vastus lateralis--light, intermediate, and dark fibers in the deep portion; and intermediate fibers with scattered dark fibers in the superficial portion. Transverse diameters varied among fibers in different portions of the quadriceps. These findings must be considered in experiments of muscle or motor endplates in hamster quadriceps muscle.
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PMID:Distribution and size of myofibers in quadriceps muscle of Syrian hamster. 744 79

Immunodominant regions of yeast plasma membrane H(+)-ATPase have been mapped by two different approaches. A rabbit polyclonal antibody was used to screen a library of random fragments of the ATPase gene in a bacterial expression plasmid. In addition, the epitopes recognized by a panel of mouse monoclonal antibodies against the ATPase were mapped by reactions with defined fragments of the enzyme expressed in Escherichia coli. Both methodologies indicated that two regions within the amino-terminal part of the ATPase (at amino acid positions 5-105 and 168-255) contain most of the antigenic determinants. The accessibility of the monoclonal antibodies to their epitopes in native and solvent-perturbed ATPase preparations was investigated by immunofluorescence studies on yeast protoplasts. Cells fixed and permeabilized with formaldehyde were either treated with or without detergents and organic solvents. ELISA competition tests with plasma membrane vesicles and with detergent-purified ATPase incubated in solution with the monoclonal antibodies gave similar results. All the epitopes were accessible in detergent-treated ATPase preparations. In contrast, only the epitopes at amino acids 24-56 were accessible in ATPase preparations not treated with detergents or organic solvents. These epitopes were cytoplasmic because protoplast permeabilization was required for decoration by the reactive monoclonal antibodies.
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PMID:Epitope mapping and accessibility of immunodominant regions of yeast plasma membrane H(+)-ATPase. 768 77

The pregnant rats were treated with formaldehyde (0.5 mg/kg daily per os) during whole period of pregnancy. The activity of cytochrome-c-oxidase, malate dehydrogenase, nucleotidase, glucose-6-phosphatase, beta-glucuronidase, N-acetyl-beta-glucosaminidase, beta-galactosidase, H(+)-ATPase, glutamate dehydrogenase, NAD- and NADP-isocitrate dehydrogenase, fructose-bisphosphate aldolase, glucose-6-phosphate dehydrogenase and content of protein in liver celts of offsprings (newborns, 2 weeks age and 2 months age) were studied. It was shown differences in development enzyme systems of control and experimental animals during ontogenesis.
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PMID:[Experimental study of the effect of formaldehyde during embryogenesis on the activity of rat liver enzyme systems in ontogenesis]. 913 53


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