Small-scale immunopurification of cytochrome c oxidase for a high-throughput multiplexing analysis of enzyme activity and amount

2007 ◽  
Vol 48 (4) ◽  
pp. 167 ◽  
Author(s):  
Birgit Schilling ◽  
James Murray ◽  
Richard H. Row ◽  
Chris B. Yoo ◽  
Bradford W. Gibson ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
High Throughput ◽  
Small Scale

scholarly journals Pulsed cytochrome c oxidase from the thermophilic bacterium PS3

1984 ◽  
Vol 223 (3) ◽  
pp. 809-813 ◽  
Author(s):  
N Sone ◽  
A Naqui ◽  
C Kumar ◽  
B Chance
Keyword(s):  
Enzyme Activity ◽  
Absorption Spectrum ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Thermophilic Bacterium ◽  
Decay Process ◽  
Mitochondrial Enzyme ◽  
Bovine Heart ◽  
Enhanced Activity

A caa3-type terminal cytochrome c oxidase (EC 1.9.3.1) from the thermophilic bacterium PS3 containing three subunits showed conversion from resting into pulsed form. Upon pulsing (reduction and re-oxidation), the cytochrome c oxidase activity increased over 10-fold. This enhanced activity of the pulsed enzyme gradually decayed. Addition of phospholipids, necessary for the enzyme activity, did not affect this decay process. Small changes in the absorption spectrum were observed for the resting-into-pulsed transition and for H2O2 ligation to the pulsed enzyme. The e.p.r. spectrum of the resting enzyme was very similar to that of mitochondrial enzyme, but the transient g = 5, 1.78 and 1.69 set of e.p.r. signals, associated with the pulsed bovine heart oxidase, were not observed in the case of pulsed bacterium-PS3 enzyme.

scholarly journals Cytochrome c oxidase subunit 4 isoform 2‐knockout mice show reduced enzyme activity, airway hyporeactivity, and lung pathology

2012 ◽  
Vol 26 (9) ◽  
pp. 3916-3930 ◽  
Author(s):  
Maik Hüttemann ◽  
Icksoo Lee ◽  
Xiufeng Gao ◽  
Petr Pecina ◽  
Alena Pecinova ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Knockout Mice ◽  
Lung Pathology ◽  
Oxidase Subunit

scholarly journals Enzyme Activity of the Cytochrome System of the Egg and Larva of the Cattle Tick (Boophilus Microplus)

1973 ◽  
Vol 26 (2) ◽  
pp. 453 ◽  
Author(s):  
AG Shanahan ◽  
JE O'hagan
Keyword(s):  
Enzyme Activity ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Nadh Oxidase ◽  
Boophilus Microplus ◽  
Cattle Tick ◽  
Oxidase System ◽  
Cytochrome C Reductase ◽  
Nadh Cytochrome ◽  
Eggs And Larvae

The enzymatic activities of the succinate-<;ytochrome c reductase system, the NADH--cytochrome c reductase system, the NADH oxidase system, and cytochrome c oxidase were determined spectrophotometrically in particulate preparations of eggs and larvae of B. micro plus.

scholarly journals Fatty acids as modulators of cytochrome c oxidase in proteoliposomes

1996 ◽  
Vol 320 (2) ◽  
pp. 557-561 ◽  
Author(s):  
Martyn SHARPE ◽  
Ivano PERIN ◽  
John WRIGGLESWORTH ◽  
Peter NICHOLLS
Keyword(s):  
Fatty Acids ◽  
Enzyme Activity ◽  
Oleic Acid ◽  
Membrane Potential ◽  
Cytochrome C ◽  
Palmitic Acid ◽  
Cytochrome C Oxidase ◽  
Respiratory Control ◽  
Similar Concentration

The control of cytochrome c oxidase turnover in proteoliposomes by membrane potential (ΔΨ) and by pH gradient (ΔpH) is probably kinetic in nature, and inhibition by valinomycin and stimulation by nigericin indicate that ΔpH exerts a greater influence than does an equivalent ΔΨ. Oleic acid at 100 µM removes all ΔΨ and ΔpH control, whereas a similar concentration of palmitic acid increases turnover but does not completely abolish control. Valinomycin acts synergistically with both fatty acids, indicating that the latter can act as H+/K+ exchangers, but neither fatty acid alone markedly affects ΔpH, showing that they cannot fully mimic nigericin. Oleate, but not palmitate, diminishes ΔΨ, and can move electrophoretically as oleate anion. Submicromolar palmitic acid concentrations partly stimulate turnover in ΔΨ- and ΔpH-controlled proteoliposomes, as reported by Labonia, Muller and Azzi [(1988) Biochem. J. 254, 130–145], which might represent a direct effect on cytochrome c oxidase. The ubiquity of fatty acids in biological membranes suggests that these substances might be responsible for limiting respiratory control and enzyme activity in vivo.

scholarly journals Comparisons of copper deficiency states in the murine mutants blotchy and brindled. Changes in copper-dependent enzyme activity in 13-day-old mice

1986 ◽  
Vol 238 (1) ◽  
pp. 177-183 ◽  
Author(s):  
M Phillips ◽  
J Camakaris ◽  
D M Danks
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Enzyme Activity ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Oxidase Activity ◽  
Copper Concentration ◽  
Copper Deficiency ◽  
Single Temperature ◽  
Deficient Mice

The activity of two copper-dependent enzymes, cytochrome c oxidase and copper, zinc-superoxide dismutase, was determined in six tissues of age-matched (13-day-old) copper-deficient mutant and normal mice. In the two mutants ‘brindled’ and ‘blotchy’, brain, heart and skeletal muscle had significant enzyme deficiencies. Cytochrome c oxidase was more severely affected than was superoxide dismutase. In these three tissues the degree of deficiency could be correlated with decreased copper concentration; however, enzyme activity was normal in liver, kidney and lung, despite abnormal copper concentrations in these tissues. In nutritionally copper-deficient mice, all six tissues showed decreased enzyme activity, which was most marked in brain, heart and skeletal muscle, the tissues which showed enzyme deficiencies in the mutants. Analysis in vitro of cytochrome c oxidase (temperature coefficient = 2) at a single temperature was found to underestimate the deficiency of this enzyme in hypothermic copper-deficient animals. Cytochrome c oxidase deficiency may therefore be sufficiently severe in vivo to account for the clinical manifestations of copper deficiency. An injection of copper (50 micrograms of Cu+) at 7 days increased cytochrome c oxidase activity by 13 days in all deficient tissues of brindled mice, and in brain and heart from blotchy mice. However, skeletal-muscle cytochrome c oxidase in blotchy mutants did not respond to copper injection. Cytochrome c oxidase activity increased to normal in all tissues of nutritionally copper-deficient mice after copper injection, except in the liver. Hepatic enzyme activity remained severely deficient despite a liver copper concentration three times that found in copper-replete controls. Superoxide dismutase activity did not increase with treatment in either mutant, but its activity was higher than control levels in nutritionally deficient mice after injection. This difference is probably due to sequestration of copper in mutant tissue such as kidney, but a defect in the copper transport pathway to superoxide dismutase cannot be excluded.

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