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.

Effect of chronic administration of acetaldehyde by inhalation on (Na+ + K+)-activated adenosine triphosphatase activity of rat brain membranes

Toxicology ◽  
1985 ◽  
Vol 34 (4) ◽  
pp. 277-284 ◽  
Author(s):  
Eiko Shiohara ◽  
Miyoko Tsukada ◽  
Shigetoshi Chiba ◽  
Hiromi Yamazaki ◽  
Keiko Nishiguchi ◽  
...  
Keyword(s):  
Rat Brain ◽  
Adenosine Triphosphatase ◽  
Chronic Administration ◽  
Adenosine Triphosphatase Activity ◽  
Brain Membranes ◽  
Rat Brain Membranes

scholarly journals LOCALIZATION OF MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE ACTIVITY IN CULTURED HUMAN CELLS

1965 ◽  
Vol 13 (8) ◽  
pp. 647-656 ◽  
Author(s):  
EDWARD ESSNER ◽  
JØRGEN FOGH ◽  
PATRICIA FABRIZIO
Keyword(s):  
Electron Microscopy ◽  
Mitochondrial Membrane ◽  
Adenosine Triphosphatase ◽  
Cultured Cells ◽  
Enzyme Reaction ◽  
Outer Mitochondrial Membrane ◽  
Adenosine Triphosphatase Activity ◽  
Different Types ◽  
Cultured Human Cells ◽  
Membrane Reaction

Adenosine triphosphatase activity has been localized by light microscopy in the mitochondria of four different types of cultured cells using the Wachstein-Meisel lead method after brief fixation in formol-calcium. The resolutions of the method permits the study of mitochondrial size, form, number and distributions in these cultured cells. Electron microscopy shows enzyme reaction product within the mitochondrion but not on the outer mitochondrial membrane. Reaction product is also localized to the plasma membrane and its infoldings.

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 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.

Gender-based Differences in Na+–K+Adenosine Triphosphatase Activity Occur in the Microcirculation of the Diabetic Rat Brain

2001 ◽  
Vol 94 (2) ◽  
pp. 372-375 ◽  
Author(s):  
Frederick E. Sieber ◽  
Patricia Hurn ◽  
Nabil J. Alkayed ◽  
Richard J. Traystman
Keyword(s):  
Rat Brain ◽  
Adenosine Triphosphatase ◽  
Diabetic Rat ◽  
Adenosine Triphosphatase Activity ◽  
Gender Based

scholarly journals THE HISTOCHEMICAL DEMONSTRATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN MYOCARDIUM

1964 ◽  
Vol 12 (10) ◽  
pp. 740-743 ◽  
Author(s):  
N. R. NILES ◽  
J. CHAYEN ◽  
G. J. CUNNINGHAM ◽  
LUCILLE BITENSKY
Keyword(s):  
Enzymatic Activity ◽  
Adenosine Triphosphate ◽  
Adenosine Triphosphatase ◽  
Inhibitory Effect ◽  
Histochemical Demonstration ◽  
Human Myocardium ◽  
Phosphate Esters ◽  
Precise Localization ◽  
Adenosine Triphosphatase Activity

Adenosine triphosphatase has been demonstrated histochemically in rat and human myocardium. To obtain its precise localization in discrete bands, apparently corresponding to the concentration of myosin, it was necessary to modify the existing technique to obtain better preservation of unfixed tissue and maximal enzymatic activity. Thus it was necessary to increase the concentration of calcium and to effect the reaction at pH 9.4 after treatment with 2:4-dinitrophenol. The specificity of the reaction was shown by these factors, by testing with phosphate esters other than adenosine triphosphate, and by the inhibitory effect of magnesium.

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