scholarly journals MICRODETERMINATION OF CYTOCHROME OXIDASE IN RAT TISSUES BY THE OXIDATION OF N-PHENYL-p-PHENYLENEDIAMINE OR ASCORBIC ACID

1963 ◽  
Vol 11 (1) ◽  
pp. 102-107 ◽  
Author(s):  
W. PEARL ◽  
J. CASCARANO ◽  
B. W. ZWEIFACH
Keyword(s):  
Ascorbic Acid ◽  
Cytochrome Oxidase ◽  
Rat Tissues

scholarly journals Peroxidase and Cytochrome Oxidase in Rat Tissues

1958 ◽  
Vol 233 (1) ◽  
pp. 209-211 ◽  
Author(s):  
Harold A. Neufeld ◽  
A.N. Levay ◽  
Fred V. Lucas ◽  
Arlene P. Martin ◽  
Elmer Stotz
Keyword(s):  
Cytochrome Oxidase ◽  
Rat Tissues

Cytochrome oxidase and ascorbic acid in the normal and regenerating tail of the Scincid lizard, Mabuya carinata

1975 ◽  
Vol 93 (3) ◽  
pp. 411-420 ◽  
Author(s):  
A.V. Ramachandran ◽  
N. Radhakrishnan ◽  
R.V. Shah
Keyword(s):  
Ascorbic Acid ◽  
Cytochrome Oxidase

The Conformational States of Oxidized and Oxygenated Beef-Heart Cytochrome c Oxidase

1975 ◽  
Vol 53 (4) ◽  
pp. 461-466 ◽  
Author(s):  
Jack A. Kornblatt ◽  
D. I. C. Kells ◽  
G. R. Williams
Keyword(s):  
Ascorbic Acid ◽  
Cytochrome C ◽  
Cytochrome Oxidase ◽  
Cytochrome C Oxidase ◽  
Sedimentation Velocity ◽  
Beef Heart ◽  
Conformational States

1. The "oxygenated" form of cytochrome oxidase has been generated by treatment of the enzyme with ascorbic acid.2. "Oxygenated oxidase" so generated is stable over long periods (24 h).3. Sedimentation velocity experiments have shown the "oxygenated oxidase to be a less compact molecule than the oxidized.

Effect of Whole Body X-Irradiation on Ascorbic Acid of Rat Tissues.

1953 ◽  
Vol 84 (2) ◽  
pp. 470-473 ◽  
Author(s):  
H. L. Oster ◽  
A. L. Kretchmar ◽  
F. H. Bethell
Keyword(s):  
Ascorbic Acid ◽  
Whole Body ◽  
Rat Tissues ◽  
X Irradiation

COMPARATIVE EFFECTS OF ALDOSTERONE AND HEAT ACCLIMATIZATION ON OXIDATIVE ENZYMES IN RAT TISSUES

1967 ◽  
Vol 45 (4) ◽  
pp. 717-722 ◽  
Author(s):  
E. Bedrak ◽  
V. Samoiloff
Keyword(s):  
Body Weight ◽  
Heat Stress ◽  
Cytochrome Oxidase ◽  
Repeated Administration ◽  
Oxidative Enzymes ◽  
Rat Tissues ◽  
Heat Acclimatization ◽  
Marked Rise ◽  
Hot Environment ◽  
Liver And Kidney

The activities of several oxidative enzymes of liver, kidney, heart, and muscle tissue were compared in groups of rats treated with aldosterone, exposed to heat stress, and acclimatized to a hot environment. A single intraperitoneal injection of 2 μg D-aldosterone monoacetate/g body weight caused an increase in the activity of liver succinoxidase after 3 h and in kidney and heart succinoxidase after 8 h. Similarly, the activity of cytochrome oxidase was enhanced 8 h after a single injection of the mineralocorticoid. Repeated administration of 2 μg D-aldosterone monoacetate/g body weight for 16 days (chronic aldosterone) elicited a significant decrease (P < 0.05) in liver succinoxidase similar to that in heat stress (P < 0.05) and in acclimatization to a hot environment (P < 0.05). On the other hand, the activity of the succinoxidase of kidney, heart, and muscle tissues was slightly stimulated by the chronic aldosterone treatment, by heat stress, and by heat acclimatization. Although the activity of cytochrome oxidase of the liver and kidney was decreased by the chronic aldosterone treatment, heat stress, and heat acclimatization, there was a slight increase in the activity in that of heart and muscle. Most treatments elicited a marked rise in the activity of kidney xanthine oxidase (P < 0.01), whereas the enzyme activity of liver, heart, and muscle was relatively unaffected.

scholarly journals ELECTRON MICROSCOPY OF LYSOSOME-RICH FRACTIONS FROM RAT THYMUS ISOLATED BY DENSITY-GRADIENT CENTRIFUGATION BEFORE AND AFTER WHOLE-BODY X-IRRADIATION

1962 ◽  
Vol 13 (2) ◽  
pp. 253-260 ◽  
Author(s):  
Y. E. Rahman
Keyword(s):  
Electron Microscopy ◽  
Acid Phosphatase ◽  
Cytochrome Oxidase ◽  
Density Gradient ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Whole Body ◽  
Rat Tissues ◽  
Before And After ◽  
X Irradiation

Fractions from rat thymuses were isolated by sucrose density-gradient centrifugation, before and after 1000 r whole-body x-irradiation, and examined by electron microscopy. Cytochrome oxidase and acid phosphatase activities of these fractions were tested as well. Electron-opaque bodies with diameters ranging from 0.10 to 0.35 µ, with a mean of 0.25 µ, were found in fractions having high acid phosphatase activity, while the fractions rich in cytochrome oxidase consisted mostly of mitochondria. After irradiation, there was an increased ratio of dense bodies to mitochondria. These particles are considered to be lysosomes similar to those identified in other rat tissues. Their relationship to the mitochondria is discussed.

Oxygen uptake and evolution by iron porphyrin enzymes

1959 ◽  
Vol 12 (1) ◽  
pp. 47
Author(s):  
NK King ◽  
ME Winfield
Keyword(s):  
Ascorbic Acid ◽  
Carbon Atom ◽  
Oxygen Uptake ◽  
Cytochrome Oxidase ◽  
Metal Atom ◽  
Iron Porphyrin ◽  
Reduction Step ◽  
The Third ◽  
Catalase Peroxidase ◽  
Electron Deficiency

Three detailed mechanisms are considered for the catalatic decomposition of H2O2. It is shown that the first of these, akin to the earlier hypotheses for catalase action, cannot satisfy the magnetic, titrimetric, and kinetic evidence. The second mechanism involves oxidation of the FeIII porphyrin to the equivalent of FeV. The electron deficiency is distributed over the ligands so that even in the most oxidized complex the iron is in the FeIV or possibly even the FeIII state. In the third scheme it is suggested that the reduction step (in which O2 is liberated) takes place at a carbon atom, while the site of the oxidation is the metal atom as commonly supposed. The liberation of O2 from H2O2 can be catalysed by 6-coordinate ruthenium II complexes. In the catalytic cycle, the metal appears to be oxidized to Rdv, then reduced to RuII. Ethanol or ascorbic acid can substitute for H2O2 in the reduction. Evidence for H2O2 attack on the ligands is suggestive but not conclusive. A brief comment is made on the bonding of oxygen to haemoglobin and myoglobin. The accumulated evidence for the structures of catalase, peroxidase, and myoglobin complexes is utilized in a scheme for the uptake of oxygen by cytochrome oxidase.

Differences in Kinetic Properties of Cytochrome Oxidase in Mitochondria from Rat Tissues. A Comparative Study

2005 ◽  
Vol 60 (9-10) ◽  
pp. 785-791 ◽  
Author(s):  
Samir P. Patel ◽  
Surendra S. Katyare
Keyword(s):  
Enzyme Activity ◽  
Regression Analysis ◽  
Cytochrome Oxidase ◽  
System Analysis ◽  
Analysis Data ◽  
Kinetic Properties ◽  
Rat Tissues ◽  
Specific Manner ◽  
Substrate Kinetics ◽  
Donor System

Abstract Substrate kinetic properties of cytochrome oxidase in rat liver, kidney, brain and heart mitochondria were examined using ascorbate + N,N,N′,N′-tetramethyl-p-phenylenediamine (TMPD) as the electron donor system. Analysis of the substrate kinetics data revealed tissuespecific expression of kinetic components exhibiting differences with respect to Km, Vmax and Kcat/Km values. Regression analysis data suggest that the enzyme activity may be regulated in a tissue-specific manner.

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