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.

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 The adenosine triphosphatase-inhibitor content of bovine heart submitochondrial particles. Influence of the inhibitor on adenosine triphosphate-dependent reactions

1977 ◽  
Vol 162 (2) ◽  
pp. 351-357 ◽  
Author(s):  
S J Ferguson ◽  
D A Harris ◽  
G K Radda
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Type I ◽  
Type Ii ◽  
Inhibitor Protein ◽  
Isolation Method ◽  
Atpase Inhibitor ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Tightly Bound Nucleotides

1. The activity of the ATPase (adenosine triphosphatase) of phosphorylating particles prepared by sonication of bovine heart mitochondria in the presence of MgCl2 and ATP is influenced by the isolation method for the mitochondria used in the preparation of particles. Type-I particles, made from mitochondria isolated in a medium lacking succinate, have a lower ATPase activity than to Type-II particles, which are prepared from mitochondria isolated in a medium containing succinate. 2. Centrifugation under appropriate energized conditions increases the ATPase activity of Type-I particles almost to that of the Type-II particles. The ATPase activity of Type-II particles was only slightly stimulated by this procedure. These data are interpreted as indicating a higher content of the ATPase-inhibitor protein in the Type-I particles. 3. A comparison was made of the ATP-driven enhancement of 8-anilinonaphthalene-1-sulphonate fluorescence and the exchange of the endogenous tightly bound nucleotides of the ATPase in Type-I and Type-II particles. The effect of exogenous inhibitor protein on both these reactions was also studied. 4. The time-scale on which the inhibitor protein can exchange between ATPase molecules is discussed.

scholarly journals Preparation and general properties of a soluble adenosine triphosphatase from mitochondria

1967 ◽  
Vol 105 (1) ◽  
pp. 279-288 ◽  
Author(s):  
M J Selwyn
Keyword(s):  
Adenosine Triphosphatase ◽  
Metal Cations ◽  
Coupling Factor ◽  
Heart Mitochondria ◽  
Aqueous Extracts ◽  
Bivalent Metal ◽  
Adenosine Triphosphatase Activity ◽  
General Properties ◽  
Kinetics Of

1. The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0° than at 25° but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg2+ or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg2+-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg2+ activation indicate that the ATP–Mg2+ complex is the important substrate: free ATP and Mg2+ are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).

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 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.

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.

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