scholarly journals CYTOCHEMICAL LOCALIZATION OF MYOFIBRILLAR ADENOSINE TRIPHOSPHATASE ACTIVITY IN SARCOMERES OF GLYCERINATED MUSCLE BY THE CALCIUM PRECIPITATION METHOD A NOVEL CONTROL IS NEEDED TO DEMONSTRATE ARTIFACTS

1971 ◽  
Vol 19 (2) ◽  
pp. 75-84 ◽  
Author(s):  
BERNARD D. TUNIK
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Protein Concentration ◽  
Pectoralis Major Muscle ◽  
Precipitation Method ◽  
Cytochemical Localization ◽  
Adenosine Triphosphatase Activity ◽  
High Protein Concentration ◽  
Glycerinated Muscle ◽  
Calcium Precipitation

The calcium precipitation method was used in an attempt to localize myofibrillar adenosine triphosphatase (ATPase) activity within the sarcomeres of single, unfixed, glycerol-extracted fibers from the pectoralis major muscle of leghorn chicks. ATPase was apparently present in only the A-I overlap region of unshortened fibers, and was apparently present in only the contraction bands of shortened fibers. The results are shown to be self-contradictory in view of the known submicroscopic morphology of the sarcomeres. However, the usual classical controls provided no evidence of artifactual localization. In a novel control, separate solutions of calcium and phosphate were caused to diffuse simultaneously into a fiber. The resulting precipitate was localized in patterns indistinguishable from those obtained from incubation of shortened or unshortened fibers in ATP. These patterns result from the localization of precipitate in regions of high protein concentration. Caution in interpreting the results of cytochemical procedures even though controls provide no evidence of artifactual localization is urged.

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.

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.

Preparation and Properties of Trout Myosin

1966 ◽  
Vol 23 (4) ◽  
pp. 563-573 ◽  
Author(s):  
H. Buttkus
Keyword(s):  
Enzyme Activity ◽  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Protein Concentration ◽  
Sedimentation Coefficient ◽  
Acetylcholinesterase Activity ◽  
Kcal Mole ◽  
Order Process ◽  
Dorsal Muscle ◽  
First Order

Myosin from the white, dorsal muscle of trout was isolated by a modification of the method of Mackie and Connell (1964). This myosin was homogeneous in the ultracentrifuge at 5 C. The corrected sedimentation coefficient, S°20,w = 6.50, was similar to those for cod and rabbit myosin. The isolated protein had two enzymatic activities, an adenosine triphosphatase (ATPase) and an acetylcholinesterase. The rate of inactivation of the acetylcholinesterase activity at 45 C was approximately equal to the rate of inactivation of the ATPase activity at 25 C. Inactivation of the ATPase was a first-order process with respect to time and 0.6th order with respect to protein concentration. The energy of activation was 46 kcal mole−1 at pH 6.8, lower than values reported for rabbit myosin. Using the loss of enzyme activity as a measure of denaturation, trout myosin was about 23 × more stable than cod myosin, but lost its activity about 25 × more rapidly than rabbit myosin. Some of the mechanisms active in denaturing myosin are briefly discussed.

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 The rate-limiting step of the protamine-induced adenosine triphosphatase activity of adenosine triphosphate-G-actin

1979 ◽  
Vol 183 (2) ◽  
pp. 475-476 ◽  
Author(s):  
A Ferri ◽  
E Magri ◽  
E Grazi
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphate ◽  
Adenosine Triphosphatase ◽  
Adenosine Triphosphatase Activity ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting

The release of Pi from the Pi-G-actin-ADP complex is the rate-limiting step in the ATPase activity that is shown by ATP-G-actin in the presence of protamine.

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