scholarly journals INVESTIGATIONS ON THE MITOCHONDRIA OF THE HOUSEFLY, MUSCA DOMESTICA L

1954 ◽  
Vol 37 (3) ◽  
pp. 343-359 ◽  
Author(s):  
Bertram Sacktor
Keyword(s):  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Musca Domestica ◽  
Flight Muscle ◽  
Phosphate Uptake ◽  
Systematic Investigation ◽  
Appreciable Effect ◽  
Considerable Influence ◽  
Isolation Medium ◽  
Normal Morphology

It has been found that mitochondria isolated from the flight muscle of the housefly, Musca domestica, are capable of effecting oxidative phosphorylation. A systematic investigation of the factors which regulate this coupling was undertaken. It was found: 1. The molarity of the isolation medium had considerable influence on the morphology of the mitochondria. These physical alterations were associated with changes in oxidation, phosphorylation, and ATPase activity. 2. In addition to an optimum isolation medium, the normal morphology of the mitochondria needed to be further stabilized by serum albumin. 3. A "latent" ATPase activity in insect mitochondria was demonstrated. An inverse relationship was found between oxidative phosphorylation and ATPase activity. 4. Oxygen consumption and the uptake of phosphate were linear with respect to time. 5. A respiratory substrate was necessary for phosphorylation and for maintenance of spatially organized mitochondria. 6. No differences in oxygen uptake were found in the presence or absence of inorganic phosphate. 7. Magnesium was required for optimal oxidative phosphorylation. Calcium and manganese inhibited both respiration and phosphorylation. 8. The addition of cytochrome c had no effect on either oxygen or phosphate uptake. 9. ATP, ADP, or AMP were capable of participating in oxidative phosphorylation, but the glucose-hexokinase trapping system was necessary. 10. Fluoride inhibited the phosphorylation of AMP, but increased P/O when ATP was used. This stimulation was not due to the inhibition of ATPase. 11. Neither arginine nor creatine was phosphorylated. 12. The addition of other isolated fractions of flight muscle to the mitochondrial system had no appreciable effect on respiration or phosphorylation.

High efficiency of oxidative phosphorylation in mitochondria of wheat

1970 ◽  
Vol 48 (6) ◽  
pp. 692-698 ◽  
Author(s):  
Igor V. Sarkissian ◽  
Hari K. Srivastava
Keyword(s):  
Reaction Time ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Microbial Contamination ◽  
High Efficiency ◽  
Respiratory Control ◽  
Appreciable Effect ◽  
Measurable Effect ◽  
Wheat Hybrid ◽  
Stimulation Of

Mitochondria of young seedlings of a wheat hybrid 31MS × 28 exhibited high efficiency of oxidative phosphorylation. The ADP:O ratios estimated polarographically approached or were equivalent to 6, 4, and 5 with α-ketoglutarate, succinate, and malate, respectively. The respiratory control values with these substrates were about 7.5, 4.5, and 2.9. When assayed manometricafly, the P:O ratios with α-ketoglutarate as substrate and 10 min of reaction time were between 5.4 and 5.8. ADP was utilized almost exclusively in oxidative phosphorylation; microbial contamination in phosphorylating reaction mixtures had no measurable effect on oxidative phosphorylation. A concentration of 1.7 × 10−5 M 2,4-dinitrophenol had no appreciable effect on stimulation of respiration by ADP. ATPase activity was increased about 13% by dinitrophenol. It appears that high efficiency of oxidative phosphorylation is a true characteristic of the mitochondria used in this study.

Quantitative requirement for ATP for active transport in isolated renal cells

1986 ◽  
Vol 251 (1) ◽  
pp. C120-C127 ◽  
Author(s):  
N. Tessitore ◽  
L. M. Sakhrani ◽  
S. G. Massry
Keyword(s):  
Atpase Activity ◽  
Active Transport ◽  
Phosphate Uptake ◽  
Quantitative Relationship ◽  
Similar Degree ◽  
Renal Cells ◽  
Stepwise Manner ◽  
Sodium Gradient ◽  
Sodium Dependent ◽  
86Rb Influx

We investigated the quantitative relationship between cellular ATP concentration and Na+-K+-ATPase activity as measured by ouabain-sensitive 86Rb influx in rabbit proximal renal cells. Cellular ATP was reduced in a stepwise manner by rotenone (10(-7) to 10(-5) M) and was increased by 10 mM adenosine. During these maneuvers, ouabain-sensitive 86Rb influx was linearly related to cellular ATP and did not saturate up to 9.9 mM ATP. In contrast, Na+-K+-ATPase activity in membranes prepared from these cells saturated at 2.0 mM ATP at various sodium (10-100 mM) and potassium (4-100 mM) concentrations. Sodium-dependent phosphate uptake and alpha-methylglucoside (alpha-MG) uptake were both inhibited to a similar degree when cellular ATP was reduced. We conclude that 1) the ATP requirement for saturation of Na+-K+-ATPase is higher in intact renal cells than in the membranes, and 2) the uptake of phosphate and alpha-MG are similarly influenced by reduction in ATP. This effect of ATP on phosphate and AMG uptake is most likely an indirect one and is secondary to changes in the sodium gradient across the cell.

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.

scholarly journals Protein kinase C-α inhibits the repair of oxidative phosphorylation after S-(1,2-dichlorovinyl)-l-cysteine injury in renal cells

2004 ◽  
Vol 287 (1) ◽  
pp. F64-F73 ◽  
Author(s):  
Xiuli Liu ◽  
Malinda L. Godwin ◽  
Grażyna Nowak
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Mitochondrial Function ◽  
Recovery Period ◽  
Β Subunit ◽  
Atp Production ◽  
Kinase C ◽  
Mitochondrial Functions

Previously, we showed that physiological functions of renal proximal tubular cells (RPTC) do not recover following S-(1,2-dichlorovinyl)-l-cysteine (DCVC)-induced injury. This study investigated the role of protein kinase C-α (PKC-α) in the lack of repair of mitochondrial function in DCVC-injured RPTC. After DCVC exposure, basal oxygen consumption (Qo2), uncoupled Qo2, oligomycin-sensitive Qo2, F1F0-ATPase activity, and ATP production decreased, respectively, to 59, 27, 27, 57, and 68% of controls. None of these functions recovered. Mitochondrial transmembrane potential decreased 53% after DCVC injury but recovered on day 4. PKC-α was activated 4.3- and 2.5-fold on days 2 and 4, respectively, of the recovery period. Inhibition of PKC-α activation (10 nM Go6976) did not block DCVC-induced decreases in mitochondrial functions but promoted the recovery of uncoupled Qo2, oligomycin-sensitive Qo2, F1F0-ATPase activity, and ATP production. Protein levels of the catalytic β-subunit of F1F0-ATPase were not changed by DCVC or during the recovery period. Amino acid sequence analysis revealed that α-, β-, and ε-subunits of F1F0-ATPase have PKC consensus motifs. Recombinant PKC-α phosphorylated the β-subunit and decreased F1F0-ATPase activity in vitro. Serine but not threonine phosphorylation of the β-subunit was increased during late recovery following DCVC injury, and inhibition of PKC-α activation decreased this phosphorylation. We conclude that during RPTC recovery following DCVC injury, 1) PKC-α activation decreases F0F1-ATPase activity, oxidative phosphorylation, and ATP production; 2) PKC-α phosphorylates the β-subunit of F1F0-ATPase on serine residue; and 3) PKC-α does not mediate depolarization of RPTC mitochondria. This is the first report showing that PKC-α phosphorylates the catalytic subunit of F1F0-ATPase and that PKC-α plays an important role in regulating repair of mitochondrial function.

The Brittleness of Ebonite

1937 ◽  
Vol 10 (4) ◽  
pp. 778-786
Author(s):  
R. Ariano
Keyword(s):  
Mechanical Properties ◽  
Cross Section ◽  
Cross Sections ◽  
Test Specimen ◽  
The State ◽  
The Other ◽  
Appreciable Effect ◽  
Considerable Influence ◽  
Minimum Depth ◽  
The Moment

Abstract The results of tests of the brittleness of ebonite are described. Resilience is influenced chiefly by the moment of inertia of the cross section of the test-specimen, but it seems also to be affected by the form of the specimen. The state of vulcanization has considerable influence on these mechanical properties within the undercured range, but with thorough vulcanization the state of cure plays no appreciable part. Notching of test-specimens is not of great importance. It diminishes the resilience, but when the tests are compared on a basis of equal moments of inertia of the resistant cross sections, this diminution becomes inappreciable in the case of brittle ebonites. On the other hand, the shape of the notch in ebonites containing no loading ingredients does influence the resilience. With V-shaped notches, the depth of the notch and its angle of aperture influence considerably the resilience of this latter type of ebonite, and notches of minimum depth are sufficient to have an appreciable effect.

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