Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

In pig lung tissue catalase positive particles (CPs) are abundant especially in type II pneumocytes and in Clara cells. In both cell types they occur as circular, oval or elongated membrane profiles surrounding a moderately electron dense matrix lacking a crystalline core. In Clara cells and in part of type II pneumocytes they are located as individual particles without any evident morphological relation to other cell organelles. In part of type II pneumocytes 5-8 particles are forming a group and their close relation to agranular endoplasmic reticulum cisterns is evident. The particles can be purified from lung homogenates by fractionated pelleting and subsequent rate sedimentation in a sucrose gradient using a zonal rotor. The catalase rich fraction bands in the middle of the gradient whereas cytochrome oxidase and part of the acid phosphatase sediments at its heavy end. A second part of acid phosphatase stays at the light end of the gradient and--according to morphological control--seems to correspond to lamellar bodies of the type II pneumocytes. The purified catalase positive particles do not contain hydroxyacid and D-aminoacid oxidases thought to be characteristic H2O2 producing enzymes of peroxisomal systems. The buoyant density of the particles (d = 1.195 g/cm3) is lower than that of liver peroxisomes. Cytochemical controls of the peroxisomal pellets exhibit the particles partly uniformly filled with reaction product, partly irregularly stained.
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PMID:Catalase positive particles from pig lung. Biochemical preparations and morphological studies. 21 Nov 1

The activity of mitochondrial cytochrome oxidase and peroxisomal catalase in the phagolysosomes and apoptotic bodies of mucoid epithelial cells was analysed. Tissue from 2-6 day old mice was used. The activity of acid phosphatase in lysosomes was also estimated. Cytochrome oxidase was demonstrated in well-preserved mitochondria inside phagosomes. Mitochondria in cells exhibiting apoptotic death also show activity of cytochrome oxidase. The enzyme activity in swollen mitochondria ceases before the membranes of the cristae disappear completely. Apoptotic bodies are phagocytosed by sister mucoid cells and, later on, they are digested inside the cell. Phagosomes which contain already degraded mitochondria show still active catalase in sequestered peroxisomes. The acid phosphatase involved in degradation of phagocytosed material originates from endocytosed lysosomes and primary and secondary lysosomes which fuse with the membranes of phagosomes.
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PMID:Cytochemical analysis of organelle degradation in phagosomes and apoptotic cells of the mucoid epithelium of mice. 21 12

1. The metabolism of [14(-14)C]erucic acid and [U-14C]palmitic acid was studied in perfused hearts from rats fed diets containing hydrogenated marine oil, rapeseed oil or peanut oil for three weeks. 2. [14C]Erucic acid was shortened to [14C]eicosenoic acid (20 : 1, n -- 9) and [14C]oleic acid (18 : 1, n -- 9) in perfused rat hearts from all diet groups. The rapeseed oil diet caused a three-fold increase and the marine oil diet a four-fold increase in the amount of chain-shortened products recovered in heart lipids at the end of perfusion, compared to peanut oil diet. 3. The content of C16:1, C18:1 and C20:1 fatty acids was increased in heart lipids of rats fed hydrogenated marine oil or rapseed oil diet, compared to peanut oil diet. 4. Feeding hydrogenated marine oil or rapeseed oil to the rats induced a 85% increase in catalase activity, a 20% increase in the activity of cytochrome oxidase and a 30--40% increase in the content of total CoA in the heart compared to rats fed peanut oil diet. 5. It is suggested that [14(-14)C]erucic acid is shortened by the beta-oxidation system of peroxisomes in the heart. The increased chain shortening in the hearts from animals fed rapeseed oil or partially hydrogenated marine oil for three weeks may be an important part of an adaptation process.
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PMID:The effect of feeding rats with partially hydrogenated marine oil or rapeseed oil on the chain shortening of erucic acid in perfused heart. 22 34

Mitochondria were isolated from the cellular slime mold. Dictyoostelium discoideum, and partially purified by sucrose density gradient fractionation. The most purified mitochondrial fraction from the gradient contained essentially no contaminating lysosomes and minimal amounts of contaminating peroxisomes as determined by the marker enzymes N-acetyl-glucosaminidase and catalase. A mitochondrial fraction with the same amount of lysosomal and peroxisomal contamination was also isolated from cells which had been treated with ethidium bromide for 5 days. The most purified mitochondrial fraction from control and ethidium bromide-treated cells had an identical buoyant density of 1.181 to 1.182 g per ml, suggesting that treatment with the drug does not result in any drastic structural changes in the mitochondrial membrane which would affect its density. In the purified mitochondria from ethidium bromide-treated cells, the content of cytochromes a-a3 was decreased over 80% and that of cytochrome oxidase and oligomycin sensitive ATPase were reduced approximately 50%. By contrast, the specific activities of NADH and succinate dehydrogenases were identical in the purified mitochondria from control and ethidium bromide-treated cells. Previously, we had reported that the specific activities of these two enzymes had nearly doubled in whole cells maintained in ethidium bromide for a time equivalent to six or seven generations after growth had stopped (Stuchell, R. N., Weinstein, B. I., and Beattie, D. S. (1973) Fed. Eur. Biochem. Coc Lett. 37, 23-26). These results suggest that continued formation of new mitochondrial membranes, with an identical complement of succinate and NADH dehydrogenases, must occur despite the cessation of cell growth which occurs as a result of the ethidium bromide induced loss of mitochondrial enzymes. Consequently, the amount of mitochondria, or mitochondrial protein per cell, calculated from the activity of NADH and succinate dehydrogenases has increased nearly 50%. Possible models to explain the control of mitochondrial biogenesis are discussed to explain these results.
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PMID:Effects of ethidium bromide on the respiratory chain and oligomycin-sensitive adenosine triphosphatase in purified mitochondria from the cellular slime mold Dicyostelium discoideum. 23 33

During germination, Streptomyces antibioticus arthrospores passed through stages: darkening, swelling and germ tube emergence. The first stage, darkening, whose main features were a decrease in absorbance and a loss of refractility, only required exogenous divalent cations (Ca2+, Mg2+ or Fe2+) and energy that can be obtained from the spore reserves. This stage was blocked by agents that inhibit ATP formation but not by antibiotics that inhibit macromolecular synthesis. The second stage, swelling, needed an exogenous carbon source and was not blocked by mitomycin C. In this stage, the spores exhibited the highest cytochrome oxidase and catalase activities and respiratory quotient. The last stage, germ tube emergence, required additional carbon and nitrogen sources. Ammonium compounds were superior to nitrate. Dry weight remained constant during the stages of darkening and swelling, with a rapid increase from the moment of germ tube emergence. Optimum pH and temperature for germination were 8.0 and 45 degrees C, respectively. Heat treatment (55 degrees C for 10 min) had no effect on germination. The fine structure of the spore underwent important changes during germination. The wall of the swollen spore became stratified and the inner layer was continuous with the germ tube wall. Macromolecular synthesis occurred in the sequence RNA, protein and then DNA. Rifampicin, streptomycin and mitomycin C prevented synthesis when added at the start of incubation. The same effect was obtained if the addition was made during germination, except with mitomycin C which inhibited DNA, but not RNA and protein synthesis.
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PMID:Fine structure, physiology and biochemistry of arthrospore germination in Streptomyces antibioticus. 34 27

Homogenates of HTC cells have been fractionated by differential centrifugation (in four particulate fractions: N, M, L, P, and a supernatant S) or isopycnic banding in linear sucrose gradients. On this basis, the following subcellular organelles may be characterized: (i) Mitochondria, detected by cytochrome oxidase and succinodehydrogenase, are collected in the M and L fractions, and equilibrate, as a narrow band, at a median buoyant density of 1.18 g/cm3. (ii) Lysosomes, detected by the latent hydrolases beta-glycerophosphatase and N-acetyl-beta-glucosaminidase, are largely sedimented in the M and L fractions, and display a broad density distribution pattern with a median value of 1.17 g/cm3. This density is decreased or increased after cultivation of the cells in presence of Triton WR-1339 or Dextran 500, respectively. The behavior of cathepsin D is somewhat at variance with that of the two other hydrolases. (iii) Plasma membrane is tentatively detected by alkaline phosphodiesterase I. Largely recovered in the P fraction, this enzyme equilibrates at a median density close to that of the lysosomal hydrolases; the bulk of cholesterol and about half of the leucyl-2-naphthylamidase are closely associated with alkaline phosphodiesterase I; HTC cells do not contain typical 5'-nucleotidase. (iv) Catalase-bearing particles, of high buoyant density (1.22 g/cm3) are present, but 30-40% of the catalase is also found readily soluble. NADPH- and NADH: cytochrome c reductase, and RNA show more complex distributions. It is suggested that the former enzyme is associated with the endoplasmic reticulum; as in liver, NADH reductase activity is shared between the endoplasmic reticulum and the mitochondria; half of the RNA is associated with free ribosomes of polysomes. True glucose-6-phosphatase could not be detected.
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PMID:Analytical fractionation of cultured hepatoma cells (HTC cells). 56 43

Sixty-eight Haemophilus somnus strains isolated from the bovine in Canada and the U.S.A. were compared. In media enriched with 5% ovine serum, 5% bovine serum and 10% yeast extract, H. somnus fermented glucose, levulose, maltose, mannitol, mannose, sorbitol, trehalose and xylose, but failed to ferment arabinose, dulcitol, galactose, inositol, lactose, raffinose, rhamnose, salicin and sucrose. The organisms acidified litmus milk, produced cytochrome oxidase, indole and hydrogen sulfide (H(2)S) and reduced nitrates to nitrites. The motility, methyl-red, acetylmethyl-carbinol urease catalase, citrate, malonate, lysine, ornithine and arginine tests were negative. Haemophilus somnus was resistant to lincomycin, neomycin and triple sulfa, but susceptible to ampicillin, chloramphenicol, streptomycin, penicillin and tetracycline. No antigenic differences were noted between strains when tested against rabbit antisera of eight strains using agglutination, complement-fixation, immunodiffusion and counterimmunoelectrophoresis tests. Low titre cross-reactions were found in the agglutination tests with some of the anti-H. somnus rabbit sera with Actinobacillus lignieresi and Moraxella bovis. No distinct antigenic similarities to nine other species of pathogenic bacteria of animal origin were found. No difference was observed between H. somnus isolates from Ontario and those from western Canada and the U.S.A.
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PMID:A comparison of various Haemophilus somnus strains. 92 55

Superoxide dismutase is shown to affect spectral changes observed upon cytochrome c oxidase reaction with H2O2, which indicates a possibility of O2- radicals being formed in the reaction. Using DMPO as a spin trap, generation of superoxide radicals from H2O2 in the presence of cytochrome oxidase is directly demonstrated. The process is inhibited by cyanide and is not observed with a heat-denatured enzyme pointing to a specific reaction in the oxygen-reducing centre of cytochrome c oxidase. The data support a hypothesis on a catalase cycle catalyzed by cytochrome c oxidase in the presence of excess H2O2 (Vygodina and Konstantinov (1988) Ann. NY Acad. Sci., 550, 124-138): (formula: see text)
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PMID:Cytochrome oxidase-catalyzed superoxide generation from hydrogen peroxide. 131 51

Electron microscopic enzyme cytochemical reactions of Entamoeba histolytica trophozoite showed that acid phosphatase (ACP) and cytidine monophosphatase (CMPase) were located in the lysosomes. The lysosome containing enzymes were distributed in the endoplasm and beneath the plasmalemma, and the releasing enzymes by lysosomes excreted outside of the plasmalemma and caused the injury to host cells. The cytochemical positive reactions of catalase and glucose-6-phosphatase (G-6-Pase) showed that E. histolytica contains microbodies and endoplasmic reticulum. The reactive products of peroxidase (POase) were seen in the lysosome-like structure. The reactions of cytochrome oxidase (COase) and succinate dehydrogenase (SDH) were both negative, indicating that E. histolytica lacked mitochondria. The reactions of thiamine pyrophosphatase (TPPase) and nicotinamide adenine dinucleotide phosphatase (NADPase) were both negative, indicating that E. histolytica lacked Golgi body. The reactions of Na(+)-K(+)-ATPase were located on plasmalemma.
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PMID:[Electron microscopic enzyme cytochemistry of Entamoeba histolytica trophozoite]. 133 24

A comparative analysis of the phenotypic and serological properties of Carnobacterium strains associated with mortalities of cultured striped bass and channel catfish and the properties of isolates from wild brown bullhead catfish in the Chesapeake Bay area in Maryland was conducted. All of the strains were gram-positive, facultatively anaerobic, nonmotile, non-spore-forming rods occurring singly or in short chains. They did not produce cytochrome oxidase or catalase, did not reduce nitrate, failed to produce H2S, were unable to grow on acetate medium, and did not produce gas from glucose or gluconate. The temperature and salinity ranges for most of the strains were 10 to 37 degrees C and 0 to 6% NaCl, respectively. The strains all fermented mannitol and inulin and were arginine dihydrolase positive; these are typical characteristics of Carnobacterium piscicola. The carbohydrate fermentation pattern exhibited by all of the isolates with the API-50 CHL system was also very similar to that shown by C. piscicola. Acid was produced from ribose, glucose, fructose, mannose, mannitol, N-acetylglucosamine, amygdaline, arbutin, esculin, salicin, cellobiose, maltose, sucrose, trehalose, and gentiobiose. The Carnobacterium strains did not show proteolytic, lipolytic, amylolytic, or hemolytic activity. Eighteen drugs were tested; all strains proved to be resistant to chloramphenicol, gentamicin, kanamycin, streptomycin, trimethoprim, quinolones, and nitrofurans. The analysis of membrane proteins supported the phenotypic similarities, two main patterns were established, one shared by the striped bass isolates and the reference strain of C. piscicola and another shared by most of the catfish strains. However, the agglutination assays demonstrated that only one Carnobacterium strain from striped bass was serologically related to C. piscicola ATCC 35586.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Biochemical and serological characterization of Carnobacterium spp. isolated from farmed and natural populations of striped bass and catfish. 178 76


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