Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Supernatants of rat skeletal muscle homogenates were fractionated by differential centrifugation and by zonal centrifugation in sucrose density gradients. Cytochrome oxidase was employed as an enzymatic marker for locating mitochondria. The subcellular fractions were also assayed for their ability to prevent the ATP-induced contraction of myofibrils. Both the mitochondrial and microsomal fractions obtained by differential fractionation were found to be rich in such relaxing activity, and the microsomal fraction was appreciably contaminated by mitochondria. In contrast to this, when fractionation was carried out by means of zonal centrifugation (4200 RPM x 205 min. to 40,000 RPM x 60 min.), relaxing activity was found to be associated only with particles having the sedimentation characteristics of microsomes (s(20,w) estimated to be between 370 and 1880S). Relaxing activity was not detected in the regions of the gradient containing either the starting sample zone (soluble phase) or the mitochondrial peak. The microsomal relaxing particles showed negligible cytochrome oxidase activity.
J Gen Physiol 1965 May
PMID:ISOLATION OF RELAXING PARTICLES FROM RAT SKELETAL MUSCLES IN ZONAL CENTRIFUGES. 1432 85

1. The kinetics of the inactivation of photosynthesis by 2537 A in Chlorella pyrenoidosa and Scenedesmus D(1) indicate that, while the destruction process is largely a first order effect, higher order effects also occur, which become evident at low exposures. In agreement with previous observations, endogenous respiration is insensitive to exposures which inactivate photosynthesis. 2. In Scenedesmus D(1) a solid dose of ultraviolet has no more effect on the photosynthetic apparatus than a dose of equal total duration interrupted by periods of photosynthesis. Nor is any difference noted if the cells are in a different buffer, e.g. 0.05 M KH(2)PO(4), or carbonate-bicarbonate buffer 9. 3. In C. pyrenoidosa, a solid dose and an interrupted dose cause equal effects on photosynthesis when neutral phosphate buffer is used. If the ultraviolet exposure schedules are identical, equal effects are also noted in cells suspended in buffer 9, and in 0.05 M phosphate (pH 6.2). Solid exposures are, however, much more effective than interrupted exposures, when buffer 9 is used. 4. Oxygen evolution (Hill reaction), photosynthesis, and photoreduction in Scenedesmus D(1) are equally sensitive to a given dose of ultraviolet. The mechanism responsible for adaptation to hydrogen metabolism is not more sensitive to ultraviolet than is the photosynthetic mechanism. The O(2)/H(2)/CO(2) reaction in darkness is less sensitive to ultraviolet than any of the above reactions. 5. Glucose oxidation by C. pyrenoidosa, and colony formation in Scenedesmus D(1) are far more sensitive to a given dose of ultraviolet than photosynthesis in these organisms. 6. The photosynthetic apparatus of C. pyrenoidosa is more sensitive to ultraviolet than that of Scenedesmus D(1). 7. The Hill reaction in chloroplast fragments is also inactivated by 2537 A by a first order process. Exposures which inactivate this reaction completely have no effect on polyphenol oxidase, cytochrome oxidase, or catalase in the same chloroplast preparation. 8. After irradiation, the survival of photosynthesis in Scenedesmus D(1) and of the Hill reaction in chloroplast fragments are independent of the light intensity used to measure these processes. 9. No significant changes occur in the ultraviolet absorption of chloroplasts after an exposure to 2537 A, which completely inactivates the Hill reaction.
J Gen Physiol 1951 May
PMID:Some effects of 2537 A on green algae and chloroplast preparations. 1483 43

1. The "indirect" thoracic muscles of adult dipterous and hymenopterous insects consist of a unique type of muscle characterized by the presence of numerous spherical, intracytoplasmic bodies termed "sarcosomes." 2. When the muscle is teased or ground, the sarcosomes are liberated as a turbid suspension of bodies ranging from 1 to 4 micro in diameter. A method is described for the isolation of sarcosomes by a simple differential centrifugation. 3. The cytochemical, chemical, and enzymatic properties of sarcosomes were examined for the purpose of appraising their relation to the cytoplasmic bodies of other tissues. 4. Fresh sarcosomes are slowly but selectively stained by the mitochondrial reagents, Janus green B and pinacyanol. Fixed sarcosomes give a positive reaction with Regaud's mitochondrial stain. 5. Chemical analyses show that approximately 29 per cent of the dry weight of sarcosomes consists of lipids and 60 per cent of protein. Microbiological assay indicates the presence of about 1 gamma of riboflavin per milligram of nitrogen. These values resemble those reported for isolated mitochondria of vertebrate liver and kidney. 6. When examined spectroscopically the sarcosomes, like the vertebrate mitochondria, show a high titer of cytochromes a, b, and c. 7. The titer of cytochrome oxidase varies systematically with the adult age of the insect. A similar relation is observed for the enzyme catalase. 8. Isolated sarcosomes show significant titers of succinoxidase, alpha-glycerophosphate dehydrogenase, malic dehydrogenase, and pyruvic dehydrogenase. The following dehydrogenases could not be demonstrated: xanthine, phenylalanine, glycine, lactic, choline, glutamic, and alcohol. These results are compared with those previously reported for vertebrate mitochondria. 9. In view of their manifold points of biochemical similarity, it is concluded that the sarcosomes are the mitochondria of this highly specialized muscular tissue.
J Gen Physiol 1951 May
PMID:Mitochondria in the flight muscles of insects. I. Chemical composition and enzymatic content. 1483 46

The metabolism of the imaginal discs of wild type, miniature, vestigial, and four-jointed varieties of Drosophila was investigated using the Cartesian diver ultramicrorespirometer. Wild type and vestigial wing disc respiration is inhibited by cyanide and azide and thus is mediated by an iron or copper porphyrin system, presumable cytochrome-cytochrome oxidase. Respiration is also inhibited by certain hydroxynaphthoquinones, believed to inactivate some enzyme between cytochromes b and c. The respiration of the vestigial and miniature wing discs is increased to normal by the addition of ascorbic acid and to a lesser extent by p-phenylenediamine and hydroquinone, hence the cytochrome oxidase and cytochrome c systems of vestigial and miniature wing discs are normal and the effects of these genes are on enzymes below cytochrome c in the respiratory chain. The respiratory enzymes of the developing imaginal discs of insects are similar to those of a wide variety of cells from bacteria to mammals. The correlation of these biochemical findings with embryological studies of the discs is discussed.
J Gen Physiol 1948 Mar 20
PMID:Studies in biochemical genetics in Drosophila. 1890 57

1. Liver, kidney, brain, skeletal muscle, and cardiac muscle from one newborn and three adult long-snouted dolphins (Stenella plagiodon) were obtained for enzyme studies. 2. All of the dolphin tissues exhibited cytochrome oxidase, succinic dehydrogenase, and malic dehydrogenase activity. Considerable differences in the enzyme activities of the various tissues were noted, with cardiac muscle exhibiting the highest respiratory enzyme activity. The enzyme activities of dolphin tissues were lower than those of the corresponding rat tissues. 3. All of the dolphin tissues exhibited adenosine triphosphatase activity which was accelerated by magnesium and manganese but, in contrast to rat tissues, was only slightly activated by calcium. 4. Measurements of the distribution of acid-soluble phosphorus in dolphin tissues indicated that glycolysis in all of the tissues examined proceeded through the Emden-Meyerhof phosphorylation scheme. 5. The average glycogen content of dolphin skeletal muscle was 0.98 per cent as compared with 0.16 to 0.20 per cent for rat skeletal muscle. The high glycogen content of dolphin skeletal muscle indicates a ready source of substrate for glycolysis even during submergence when the blood supply may be differentially shunted to other organs. 6. Measurements of the organ weights of dolphins showed that the lungs occupy over three times and the liver one-half as much of the total body weight as do these organs in the rat. The heart and the thyroid gland of the dolphin are also larger in proportion to the total body weight than in the rat while the relative weights of the other tissues in the two species are about the same.
J Gen Physiol 1948 Mar 20
PMID:Studies on the intermediary carbohydrate metabolism of aquatic animals; the distribution of acid-soluble phosphorus and certain enzymes in dolphin tissues. 1890 58

1. Iron spicules found in the brains of general paretic patients are formed from endogenous brain iron normally present in another form. This supports our earlier view that the micro value of 16,000 obtained in advanced paretics for alpha brain wave frequencies as a measure of cortical respiration comes about from the slowing of an iron catalyzed link in cortical respiration such as would result from the reduction of available cytochrome and its oxidase, thus making this step a chemical pacemaker. 2. To test the basic theory of chemical pacemakers, a study was made of the succinate-fumarate enzyme system containing succino-dehydrogenase and cytochrome-cytochrome oxidase acting sequentially. 3. The micro value for the unpoisoned system is 11,200 +/- 200 calories. 4. According to theory, the addition of a critical amount of cyanide known to be a specific poison of the cytochrome-cytochrome oxidase system (and not of the dehydrogenase) should shift the micro cleanly to 16,000 calories, and it does. 5. According to theory, selenite, a specific poison for the dehydrogenase, should stop all respiration without shifting the micro. This also is found to be the case. 6. The theory also predicts that if the micro is shifted from 11,000 +/- to 16,000 +/- by cyanide, the subsequent addition of a critical amount of selenite should shift the micro back again to 11,000 +/- calories, and this is found to occur. 7. It is concluded that approximately 11,000 calories is the energy of activation of the succino-dehydrogenase-catalyzed step and 16,000 calories is that for the cytochrome-cytochrome oxidase-catalyzed step. These two values are encountered more frequently than any others in physiological systems. It is to be recalled that a shift of micro for alpha brain wave frequencies from 11,000 to 16,000 calories occurs in the course of advancing syphilitic brain infection and is accompanied by a change in form of brain iron.
J Gen Physiol 1939 Sep 20
PMID:CHEMICAL PACEMAKERS : PART I. CATALYTIC BRAIN IRON. PART II. ACTIVATION ENERGIES OF CHEMICAL PACEMAKERS. 1987 42

1. In a previous paper it was found that 11,200 calories is obtained for the energy of activation in the oxidation of succinate to fumarate in the presence of crude beef heart extract when succino-dehydrogenase was made the limiting factor. 16,000 calories was obtained with this preparation when cytochrome-cytochrome oxidase was made the limiting factor. In the present paper activation energies of the components of this enzyme system are further studied. 2. Oxidation of p-phenylenediamine catalyzed by the extract and known not to involve the dehydrogenase component yields Arrhenius equation plots indicating a pacemaker reaction with a micro of 9,500 calories. 3. An activation energy of 17,500 calories is obtained for the oxidation of succinate to fumarate in the presence of the beef heart extract partially poisoned by pyrophosphate. Evidence is presented that this value corresponds to a link in the respiratory chain other than that of succino-dehydrogenase or cytochrome c-cytochrome oxidase. 4. Addition of a suitable amount of cresyl blue to a beef heart extract reaction mixture, completely inhibited by cyanide, restores the oxidation of succinate to normal in the presence of pure oxygen. In this system, in which the dye is substituted for the oxidase, when the enzyme extract (dehydrogenase) is made the limiting factor, a micro of 18,500 calories is obtained; when cresyl blue is made the limiting factor, the micro value is 22,000 calories. 5. Results of these experiments indicate that energies of activation are associated not with the enzyme as such, but with the particular reaction steps involving them as catalysts.
J Gen Physiol 1941 Jan 20
PMID:CHEMICAL PACEMAKERS : III. ACTIVATION ENERGIES OF SOME RATE-LIMITING COMPONENTS OF RESPIRATORY SYSTEMS. 1987 20

1. An enzyme capable of oxidizing reduced cytochrome c (i.e. a cytochrome oxidase) has been obtained from Arbacia eggs. In 0.02 M hydroquinone, the cytochrome oxidase was half activated at a cytochrome c concentration of approximately 4 x 10(-6)M. The concentration of the cytochrome oxidase was found to be nearly the same in unfertilized and fertilized eggs, the amount of the enzyme-as measured by means of its activity toward cytochrome c as a representative substrate-being more than sufficient to account for the highest rate of oxygen utilization yet observed in the intact, living, fertilized eggs, and of the same order as that in certain rat tissues. 2. The Arbacia cytochrome oxidase was strongly inhibited by carbon monoxide in the dark, the inhibition being almost completely reversed by light. The inhibition constant was not greatly altered by variation in the concentration of cytochrome c or the concentration of hydroquinone used as reductant for the cytochrome c, having a value of 3 to 5 under the conditions used. The inhibition constant was about 2 with p-phenylenediamine as reductant for the cytochrome c, but apparently had the surprisingly low value of about 0.5 with 0.02 M cysteine as reductant. 3. The cytochrome oxidase was completely inhibited by sufficiently high concentrations of sodium cyanide, sodium azide, and sodium sulfide. It was also completely inhibited in 0.6 M sodium chloride. It was not inhibited by two inhibitors of copper containing enzymes, 8-hydroxyquinoline and sodium diethyldithiocarbamate. It was also not significantly inhibited by 2,4-dinitrothymol, 2,4-dinitro-o-cyclohexylphenol, phenylurethane, 5-isoamyl-5-ethylbarbituric acid, or iodoacetic acid. 4. Quantitative examination of the fertilized eggs showed that cytochrome c, if present at all, occurred in a concentration of less than 2 micrograms per gram of wet fertilized Arbacia eggs. On the basis of these data and those of Fig. 2, above, it seems safe to conclude that cytochrome c cannot carry a significant fraction of the oxygen consumption of fertilized Arbacia eggs. It was also found that, in contrast to similar preparations from certain other animal tissues, the Arbacia cytochrome oxidase preparation displayed no succinic dehydrogenase activity when tested manometrically in the presence of excess cytochrome c. 5. Extending previously reported (3) experiments with other inhibitors, the effects of sodium azide and sodium sulfide on the respiration and cell division of fertilized Arbacia eggs were determined, the eggs being initially exposed to the reagents 30 minutes after fertilization at 20 degrees C. With either reagent cleavage was completely blocked by a concentration of reagent which reduced the respiration to approximately 50 per cent of the normal level. 6. On the basis of certain theoretical considerations regarding the possible mechanism of action of cyanide and other respiratory inhibitors it is suggested that a fraction of the respiration apparently concerned with supplying energy for division processes in the fertilized Arbacia egg may be keyed into the respiratory cycle through a carrier having a somewhat higher potential than those which carry the larger portion of the egg respiration. The theory is also employed in an effort to resolve a number of hitherto apparently paradoxical observations regarding the effects of cyanide, azide, and carbon monoxide on cell respiration.
J Gen Physiol 1941 May 20
PMID:STUDIES ON CELL METABOLISM AND CELL DIVISION : V. CYTOCHROME OXIDASE ACTIVITY IN THE EGGS OF ARBACIA PUNCTULATA. 1987 37

Aerobic respiration of Streptococcus pyogenes and pneumococcus Type 1 are strongly inhibited by KCN, NaN(3), and Na(2)S. The anaerobic glycolysis of glucose by pneumococcus is also inhibited by KCN and NaN(3). Streptococcus pyogenes, E. coli, pneumococcus Type 1, B. subtilis, B. proteus, and Staphylococcus aureus did not catalyze the oxygen uptake by p-phenylenediamine in the presence of added cytochrome c or in its absence. Yeast cells, B. subtilis, and B. pyocyaneus oxidized p-phenylenediamine to a dark purple meriquinoid substance in contrast to the other bacteria mentioned above. Streptococcus pyogenes in contrast to pneumococcus Type 1 catalyzed the oxygen uptake by cysteine. Neither of these bacteria catalyzed the oxygen uptake by tyrosine, adrenaline, pyrocatechin, xanthine, and hypoxanthine. Streptococcus pyogenes, pneumococcus Type 1, and E. coli, boiled and not boiled, gave positive peroxidative tests with benzidine showing the presence of hematin compounds. The results discussed in the light of the interpretations offered by Keilin and Harpley show that Streptococcus pyogenes and pneumococcus Type 1 contain cyanide-sensitive respiratory systems which are different from the cytochrome c-cytochrome oxidase system.
J Gen Physiol 1942 Sep 20
PMID:CYANIDE-SENSITIVE BACTERIAL RESPIRATORY SYSTEMS DIFFERENT FROM THE USUAL CYTOCHROME-CYTOCHROME OXIDASE SYSTEM. 1987 23

The inhibitors usually associated with the activity of the cytochrome oxidase system-cyanide and carbon monoxide-are also effective in reducing the oxidation of H(2) by intact cells of Azotobacter vinelandii. The hydrogenase system is more sensitive to CO than is the respiratory system. Oxidation of a carbon source and of hydrogen by Azotobacter cells is inhibited in a quantitatively different manner by the following compounds: sodium azide, hydroxylamine, sodium iodoacetate, and sodium fluoride. In every case, a concentration range which is definitely inhibitory for respiration has little or no effect on the hydrogenase activity. The differential inhibition by hydroxylamine explains certain observations in the literature which have been erroneously interpreted as demonstrating a specific inhibition by NH(2)OH of biological nitrogen fixation. This supposed demonstration has been offered as support for the hypothesis that NH(2)OH is an intermediate in the fixation reaction. The differential inhibitors can be used for detection of hydrogenase in cultures possessing a high endogenous respiration. The method is illustrated by an experiment with root nodule bacteria from pea and cowpea nodules. No hydrogenase was found in either.
J Gen Physiol 1943 Jan 20
PMID:ACTION OF INHIBITORS ON HYDROGENASE IN AZOTOBACTER. 1987 42


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