scholarly journals ADENOSINE TRIPHOSPHATASE: A NEUROHISTOCHEMICAL STUDY

1962 ◽  
Vol 10 (6) ◽  
pp. 731-740 ◽  
Author(s):  
D. NAIDOO
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Wistar Rat ◽  
The Other ◽  
Nuclear Staining ◽  
Adenosine Triphosphatase Activity ◽  
Bivalent Cations ◽  
Vascular Elements ◽  
The Brain ◽  
Cerebral Vascular

The location of adenosine triphosphatase in the brain has been studied in rapidly frozen-dried cerebral tissues of the Wistar rat. It is found that adenosine triphosphatase is an almost exclusively nuclear enzyme. Two tissue fractions of the cerebrum were separated, so that one sample was made up of vascular elements, and the other of neural elements. The two fractions were then studied for their adenosine triphosphatase activity, and compared with the histochemical findings. The two tissue fractions were found not to differ in the absence of bivalent cations. When Ca++ were added to the cerebral vascular suspension, ATPase activity was increased approximately 15 times, and only 3 times in the presence of Mg++. Conversely, the addition of Mg++ increased the ATPase activity of the neural fraction 200%; whereas, Ca++ was responsible for a 60% increase. This fact was detectable microscopically when Ca++ was found to intensify vascular nuclear staining, and Mg++ to increase the neuronal and glial nuclear staining. The results, histochemical and biochemical, are mutually confirmatory.

scholarly journals Partial diploids of Escherichia coli carrying normal and mutant alleles affecting oxidative phosphorylation

1977 ◽  
Vol 162 (3) ◽  
pp. 665-670 ◽  
Author(s):  
F Gibson ◽  
G B Cox ◽  
J A Downie ◽  
J Radik
Keyword(s):  
Escherichia Coli ◽  
Fluorescence Quenching ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Growth Yields ◽  
Normal Allele ◽  
Adenosine Triphosphatase Activity

A plasmid was isolated which included the region of the Escherichia coli chromosome carrying the known genes concerned with oxidative phosphorylation (unc genes). This plasmid was used to prepare partial diploids carrying normal unc alleles on the episome and one of the three mutant alleles (unc A401, uncB402 or unc-405) on the chromosome. These strains were compared with segregants from which the plasmid had been lost. Dominance of either normal ormutant unc alleles was determined by growth on succinate, growth yields on glucose, Mg-ATPase (Mg2+-stimulated adenosine triphosphatase) activity, atebrin-fluorescence quenching, ATP-dependent transhydrogenase activity and oxidative phosphorylation. In all the above tests, dominance of the normal allele was observed. However, in membranes from the diploid strains which carried a normal allele and either of the mutant alleles affecting Mg-ATPase activity (uncA401 or unc-405), the energy-linked functions were only partially restored.

Effect of Electroconvulsive Therapy on Erythrocyte Adenosine Triphosphatase Activity in Depressive Illness

1980 ◽  
Vol 137 (4) ◽  
pp. 343-345 ◽  
Author(s):  
L. J. Whalley ◽  
M. Scott ◽  
H. W. Reading ◽  
J. E. Christie
Keyword(s):  
Atpase Activity ◽  
Erythrocyte Membrane ◽  
Electroconvulsive Therapy ◽  
Healthy Subjects ◽  
Adenosine Triphosphatase ◽  
Depressive Illness ◽  
Slight Reduction ◽  
Acute Effects ◽  
Adenosine Triphosphatase Activity ◽  
Depressed Patients

SummaryErythrocyte membrane adenosine triphosphatase activities were examined in twelve unipolar depressed patients receiving ECT. Eleven patients undergoing diagnostic cystoscopy served as controls for the acute effects of anaesthesia, and sixteen healthy subjects served as non-depressed controls. The unipolar depressed patients had a slight reduction in their (Na++K+)-ATPase activity but effective ECT treatment was not associated with any increase in this activity. This approach is unlikely to cast further light on the membrane phenomenology of depressive illness.

scholarly journals Involvement of the endogenous inhibitor protein in the MgATP-induced inhibition of soluble mitochondrial adenosine triphosphatase activity

1981 ◽  
Vol 200 (3) ◽  
pp. 655-661 ◽  
Author(s):  
P N Lowe ◽  
R B Beechey
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Heart Mitochondria ◽  
Inhibitor Protein ◽  
Endogenous Inhibitor ◽  
Adenosine Triphosphatase Activity

Chloroform-released ATPase from ox heart mitochondria contains significant amounts of inhibitor protein. There is a correlation between processes that affect the interactions between the inhibitor protein and the ATPase molecule and the ability of MgATP to induce an inhibition of ATPase activity. Evidence is presented suggesting that the endogenous inhibitor protein is involved in the process of MgATP-induced inhibition of soluble ATPase activity.

Defective Membrane Systems in Dystrophic Skeletal Muscle of the UM-X7.1 Strain of Genetically Myopathic Hamster

1975 ◽  
Vol 49 (4) ◽  
pp. 359-368
Author(s):  
N. S. Dhalla ◽  
A. Singh ◽  
S. L. Lee ◽  
M. B. Anand ◽  
A. M. Bernatsky ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Atpase Activity ◽  
Calcium Binding ◽  
Adenosine Triphosphatase ◽  
Calcium Uptake ◽  
Initial Rate ◽  
The Other ◽  
Membrane Systems ◽  
Dystrophic Muscle ◽  
Mitochondrial Calcium Uptake

1. The function of mitochondria, sarcotubular membranes (heavy microsomes), sarcolemma and myofibrils from the hind-leg skeletal muscle of about 60- and 150-day-old normal and myopathic (UM-X7.1) hamsters was examined. 2. The mitochondrial calcium uptake as well as mitochondrial phosphorylation and respiratory rates were lower in 60-day-old myopathic skeletal muscle, unlike 150-day-old myopathic animals, when pyruvate-malate and glutamate-malate were used as substrates. However, mitochondria from 150-day-old myopathic animals showed depressed glutamate-dependent respiratory and phosphorylation rates and succinate-supported initial rate of calcium uptake. 3. The microsomal calcium-uptake, but not calcium-binding, and Ca2+-stimulated adenosine triphosphatase (ATPase) activity of the 150-day-old myopathic skeletal muscle were lower than the control values. Although microsomal calcium-binding, calcium-uptake and ATPase activities of the 60-day-old myopathic muscle were not depressed significantly, the initial rate of calcium uptake was less than the control. 4. The sarcolemmal Ca2+-ATPase, but not Mg2+-ATPase or Na+ +K+-ATPase, activity was higher in 60-day-old myopathic muscle whereas the activities of all these enzymes from 150-day-old myopathic animals were higher than the control. On the other hand, the Na+ +K+-ATPase activities from 60- and 150-day-old myopathic animals were inhibited by ouabain to a lesser extent in comparison with the respective control values. 5. The myofibrillar Ca2+-ATPase and Mg2+-ATPase activities as well as inhibition of Mg2+-ATPase due to Na+ and K+ in myopathic muscle were no different from the control values. 6. The results reported here give further support to the view that different membrane systems of the dystrophic muscle are defective.

The histochemical demonstration of myofibrillar adenosine triphosphatase activity in fish muscle

1974 ◽  
Vol 52 (7) ◽  
pp. 871-877 ◽  
Author(s):  
I. A. Johnston ◽  
S. Patterson ◽  
P. Ward ◽  
G. Goldspink
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Fish Muscle ◽  
Histochemical Demonstration ◽  
Differential Staining ◽  
Fiber Types ◽  
Myofibrillar Atpase ◽  
Adenosine Triphosphatase Activity ◽  
Acid Ph ◽  
Myofibrillar Atpase Activity

A technique for the demonstration of myofibrillar adenosine triphosphatase activity (ATPase) used for mammalian muscle has been modified to suit fish muscle. The mammalian method involves selectively inhibiting fiber types by preincubation at either alkaline (pH 10.4) or acid (pH 4.3) pH before incubation for myofibrillar (ATPase) activity. Fish muscle fibers were found to be generally inactivated under these conditions. Preincubation at an acid pH was found to be unsuitable for fish muscle because of the indiscriminate inactivation of the fibers. The effects of preincubating at pH 10.4 and incubating tissue sections for different time periods and at different pH's and temperatures have been investigated. A differential staining of fiber types correlated with biochemical data on myofibrillar ATPase for red and white muscles was obtained by preincubating sections for short periods (1–2 min) at pH 10.4. Under these conditions the intermediately positioned pink fibers were found to stain similarly to the white fibers of high myofibrillar ATPase activity. An investigation has been made of the qualitative distribution of fiber types in the myotomal muscle of live teleost species: coalfish (Gadus virens), grey mullet (Mugil cephalus), crucian carp (Carassius carassius), black mollie (Mollienesia sp), and glassfish (Chanda ranga). The pink fibers were found to be abundant in all the species examined with the exception of the glassfish.

scholarly journals Temperature-dependence of activation and inhibition of rat-brain adenosine triphosphatase activated by sodium and potassium ions

1966 ◽  
Vol 100 (3) ◽  
pp. 762-767 ◽  
Author(s):  
N Gruener ◽  
Y Avi-Dor
Keyword(s):  
Rat Brain ◽  
Adenosine Triphosphatase ◽  
Arrhenius Plot ◽  
Enzyme System ◽  
The Other ◽  
Potassium Ions ◽  
Adenosine Triphosphatase Activity ◽  
Brain Microsomes ◽  
High Concentrations ◽  
Sodium And Potassium

1. The adenosine-triphosphatase activity of rat-brain microsomes was measured between 0 degrees and 37 degrees . The stimulatory effect of Na(+) plus K(+) on the Mg(2+)-dependent adenosine-triphosphatase activity decreased sharply with decreasing temperature and became negligible at 0 degrees . An Arrhenius plot drawn from the experimental data showed two discontinuities: one at about 6 degrees and the other at about 20 degrees . 2. The increment in activity induced by Na(+) plus K(+) was more sensitive to oligomycin at lower than at higher temperatures, but the opposite was observed for ouabain. The action of oligomycin showed a biphasic character, since below a certain concentration it caused slight activation of Na(+)-plus-K(+)-activated adenosine triphosphatase. 3. Where oligomycin increased the activity of the enzyme, it also enhanced the accumulation of an acid-precipitable phosphorylated compound formed through the transfer of the gamma-phosphate group of [(32)P]ATP to the enzyme system. Stimulatory concentrations of oligomycin did not interfere with K(+)-mediated dephosphorylation of the intermediate, though high concentrations of oligomycin counteracted the effect of K(+). 4. The temperature profile of K(+)-stimulated microsomal phosphatase qualitatively resembled that of microsomal adenosine triphosphatase.

Localization of adenosine triphosphatase activity in motile bacteria

1973 ◽  
Vol 19 (10) ◽  
pp. 1265-1267 ◽  
Author(s):  
Z. Vaituzis
Keyword(s):  
Escherichia Coli ◽  
Atpase Activity ◽  
Uniform Distribution ◽  
Adenosine Triphosphatase ◽  
Periplasmic Space ◽  
Reaction Products ◽  
Adenosine Triphosphatase Activity ◽  
Atpase Reaction ◽  
Motile Bacteria

Cytochemical studies on motile bacteria revealed magnesium-dependent adenosine triphosphatase (ATPase) activity at the membranous sites of flagellar origin. The studies were done on bacteria representing three types of flagellation, namely, peritrichate, lophotrichate, and monotrichate. Escherichia coli and S. serpens showed a uniform distribution of ATPase reaction products throughout the periplasmic space. In B. licheniformis and V. metchnikovii the reaction products were found in the cytoplasm accumulated in areas where flagella originate.

scholarly journals HISTOCHEMICAL DEMONSTRATION OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE ACTIVITY IN TISSUE SECTIONS

1962 ◽  
Vol 10 (1) ◽  
pp. 65-74 ◽  
Author(s):  
MAX WACHSTEIN ◽  
MAIRE BRADSHAW ◽  
JOSÉ M. ORTIZ
Keyword(s):  
Adenosine Triphosphatase ◽  
Histochemical Demonstration ◽  
The Other ◽  
Mitochondrial Activity ◽  
Bile Canaliculi ◽  
Adenosine Triphosphatase Activity ◽  
Tissue Sections ◽  
Dog Kidney ◽  
Cryostat Sections ◽  
Neutral Formalin

A comparative study was made of the distribution of mitochondrial adenosine triphosphatase activity in several organs of rat and rabbit using both the calcium and lead techniques. Certain modifications in these techniques assured both improved intracellular morphology and considerable preservation of enzyme activity. Of particular importance was the low temperature (–2 to –3°C) of the neutral calcium-formol solution, and, following short fixation (lead method), a subsequent wash in neutral buffer. Mitochondrial activity was similar with both techniques, but the lead method proved to be less costly, less time-consuming, and above all, far less capricious than the calcium technique. In good preparations, the appearance of mitochondria is as clearly defined as in sections stained with non-enzymatic, conventional techniques. Long exposure of cryostat sections to formalin or preparation of sections from tissue blocks fixed in neutral formalin leads to the complete abolition of mitochondrial activity; on the other hand, it accentuates enzyme staining of other structures, such as, for instance, bile canaliculi in the liver and the secretory capillaries in the pancreas and salivary glands. It also visualizes the infolding membranes in certain tubules of the rat and dog kidney. It is assumed that formalin-fixation aids in the enzymato-morphologic distinction of these two different intracellular structures.

Advanced Photoperiod and Water Temperature Effects on Gill Na+–K+ Adenosine Triphosphatase Activity and Migration of Juvenile Steelhead (Salmo gairdneri)

1981 ◽  
Vol 38 (7) ◽  
pp. 758-764 ◽  
Author(s):  
W. S. Zaugg
Keyword(s):  
Atpase Activity ◽  
Temperature Effects ◽  
Adenosine Triphosphatase ◽  
Salmo Gairdneri ◽  
Migratory Behavior ◽  
Fish Hatchery ◽  
Adenosine Triphosphatase Activity ◽  
Migratory Season ◽  
And Migration ◽  
Migratory Movements

Under raceway conditions, an advanced photoperiod schedule caused migratory movements and elevation in gill Na+–K+ adenosine triphosphatase activity (Na+–K+ ATPase) to occur about 1 mo earlier than normal in yearling summer steelhead (Salmo gairdneri) from Dworshak National Fish Hatchery (Idaho). Exposure of migrants to 13 °C for 20 d resulted in serious impairment of continued migratory behavior and a reduction of gill Na+–K+ ATPase activity. Migrants outnumbered nonmigrants at fork lengths of 16 cm and longer. It is proposed that the potentially detrimental effects of warming river temperatures during the normal migratory season and delayed migration caused by dams and impoundments might be partially overcome by inducing early smolt transformation and migration with the use of advanced photoperiods.Key words: ATPase, steelhead, migration, temperature, photoperiod, smolts

scholarly journals ADENOSINE TRIPHOSPHATASE ACTIVITY IN RAT BRAIN FOLLOWING DIFFERENTIAL FIXATION WITH FORMALDEHYDE, GLUTARALDEHYDE, AND HYDROXYADIPALDEHYDE

1965 ◽  
Vol 13 (3) ◽  
pp. 191-205 ◽  
Author(s):  
RICHARD M. TORACK
Keyword(s):  
Electron Microscopy ◽  
Enzymatic Activity ◽  
Rat Brain ◽  
Adenosine Triphosphatase ◽  
Physiological Activity ◽  
Formalin Fixation ◽  
Adenosine Triphosphatase Activity ◽  
Chemical Inhibition ◽  
Rat Cerebrum ◽  
The Brain

Differential fixation of rat brain has been described using formaldehyde, glutaraldehyde and hydroxyadipaldehyde by perfusion or prolonged immersion. Fixation by prolonged immersion appears preferable since it produces a similar result with greater simplicity. Distribution of reaction product resulting from adenosine triphosphate hydrolysis in these fixed brains appears different and characteristic for each of these fixatives when they are used in this manner. More adenosine triphosphatase activity in rat brain was observed following formalin fixation than after fixation with either glutaraldehyde on hydroxyadipaldehyde; in this respect formalin fixation is recommended for over-all study of adenosine triphosphatase activity in the brain. The use of glutaraldehyde and hydroxyadipaldehyde seems indicated when study of enzymes surviving these fixatives is desired. Beside varying inactivation by different aldehyde fixatives, adenosine triphosphatase activity of rat brain has been characterized by distinct substrate preference and by chemical inhibition. Specificity of adenosine triphosphatase localization in rat cerebrum by electron microscopy seems enhanced by such differential fixation since differences in enzymatic activity not previously apparent can he recognized in closely related structures such as components of the blood-brain barrier. Since adenosine triphosphatase activity of astroglia in corpus callosum as well as in subpial and subependymal glial networks is glutaraldehyde resistant, an enzymatic similarity perhaps related to their physiological activity is indicated in these cells. Astroglia of cortex evince enzyme activity that survives only formalin fixation, suggesting a different function for cortical astrocytes. The enzymatic activity of oligodendrocytes appears to be a diphosphatase inactivated by glutaraldehyde and hydroxyadipaldehyde, and in this is strikingly similar to diphosphatase of Golgi apparatus.

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