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

Mitochondria were isolated from the heme-requiring insect trypanosomatid, Crithidia fasciculata, which had respiratory activity, showed a P/O ratio with succinate of 0.5 to 1.0, and contained 40 to 50% of the heme a and heme c found in the intact cells. Cytochromes b, c(555), possibly c(1), cytochrome oxidase, a carbon monoxide-binding pigment, and flavoproteins were detectable in the spectra of both intact cells and mitochondria. Cytochrome c(555) is a basic protein that was extracted from cells and mitochondria with salt solutions. The molar ratio of heme c to heme a was approximately 2:1 in both cells and mitochondria. This organism could possibly serve as a model for studies of the respiratory activity of the pathogenic trypanosomes.
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PMID:Respiratory pigments of Crithidia fasciculata. 566 93

Toyopearl media for gel filtration tend to adsorb proteins at high ionic strength, presumably by hydrogen bonding. This is used in the technique proposed here for resolution of crude protein mixtures and initial purification of their components. Proteins can be selectively adsorbed on a column of Toyopearl at high ammonium sulfate concentration and then eluted by decreasing the salt concentration. This single-step procedure can replace the usual salt fractionation of protein mixtures, which is demonstrated with yeast cytochrome oxidase.
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PMID:Adsorption chromatography on Toyopearl: a single-step alternative to salt fractionation of protein mixtures. 609 56

Severe copper deficiency was induced in rats by rearing nursing dams and their offsprings on a semisynthetic diet comprising all the requisite nutrients and trace metals except copper. The copper-deprived rats exhibited growth retardation, severe anaemia, loss of caeruloplasmin, decrease of cytochrome oxidase, accumulation of salt-soluble collagen and a drastic decrease in iron in plasma and liver. Apart from these characteristic signs of deficiency, a marked inhibition of protein synthesis was found to occur both in vivo and in cell-free liver preparations. The curtailed ability to carry out endogenously coded amino acid incorporation into protein contrasted with the unimpaired poly(U)-acid-directed phenylalanine polymerization. This inhibition pattern, as well as the attendant disaggregation of the liver polyribosomes, suggested that the primary biosynthetic lesion was located at the stage of peptide-chain initiation. Concurrently with this alteration there was a pronounced depletion of the hepatic ATP content, associated with a parallel depression of mitochondrial respiration and an enhancement of ATPase activity. Supplementation of the copper-deficient diet with a 2-4-fold excess of iron (relative to the standard diet) prevented growth retardation and anaemia and restored normal energy metabolism, as well as unimpaired protein-synthesizing capacity. The conclusion that these disturbances were primarily determined by the secondary iron deficiency was also borne out by the finding that similar alterations occurred in rats maintained on a copper-sufficient but iron-deficient diet. On the other hand, the iron-fortified diet failed to reverse the other signs of copper deficiency, namely the loss of caeruloplasmin, the diminished rate of cytochrome oxidase and the increase of soluble collagen. The interrelations between the various biochemical lesions induced by deprivation of copper or iron are discussed and the possible role of ATP depletion in determining the derangement of protein synthesis is considered.
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PMID:Biochemical lesions in copper-deficient rats caused by secondary iron deficiency. Derangement of protein synthesis and impairment of energy metabolism. 625 58

Cytochrome oxidase has been resolved in acetic acid and high salt/detergent media. In 0.5% acetic acid, the smaller subunits of the enzyme are selectively extracted with retention of an insoluble protein fraction containing subunits I-IV, VII. This fraction retains all the heme and copper of the original enzyme in a spectrally unaltered state, and possesses enzymic activity comparable to the unresolved enzyme. The further removal of subunit IV from this fraction results in migration of heme and copper and modification of their spectral characteristics. Resolution of the enzyme in a high salt/detergent medium extracts smaller subunits (V-VII) together with subunit IV and some heme and copper. The heme associated with this enzymically active extract has spectral characteristics that are partially suggestive of heme a3. It is suggested that the fraction of subunits I-IV,VII, resolved in dilute acetic acid, may represent the limit of resolution of the cytochrome oxidase complex that remains actively and spectrally indistinguishable from the original enzyme.
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PMID:Studies on the resolution of cytochrome oxidase. 626 95

The synthesis of a series of amphipathic nitroxide lipid spin labels is reported. Thus, 12-proxylhexadecanol has been converted into the versatile fatty acid spin label 14-proxylstearic acid. This substance was used to prepare 14-proxylstearyltrimethylammonium methanesulfonate, a positively charged label, and 14-proxylstearylmethyl phosphate sodium salt, a negatively charged label. Also prepared in the doxyl series were quaternary ammonium salts derived from 16-doxyl- and 7-doxylstearic acid. The positively charged and negatively charged proxyl labels were used in a preliminary experiment to investigate the role of charge in their interaction with reconstituted cytochrome oxidase. The average binding affinity of the negatively charged label is approximately 2-fold higher than that of the positively charged label at pH 7.4. At pH 5.5 the average relative affinity for negatively charged label is about 3.5-fold higher than that of positively charged label, suggesting that the ionizable group(s) on the protein can interact with the lipid headgroup.
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PMID:Synthesis of charged amphipathic nitroxide lipid spin labels and an example of their application in membrane studies. 629 18

The interaction between the oxidized forms of cytochrome c and cytochrome c oxidase (EC 1.9.3.1) has been investigated by 1H-NMR longitudinal relaxation measurements. It is found that relaxation of methyl groups on the heme ring of cytochrome c markedly deviates from a simple exponential behavior in the presence of small amounts of cytochrome oxidase. A comparison with the relaxation behavior of cytochrome c modified by 4-carboxy-3,5-dinitrophenyl at Lys-13 shows that the oxidase induces a conformation in native cytochrome c that is closely related to that of the derivative. It is suggested that this change in conformation consists of a rupture of the salt bridge between Lys-13 and Glu-90 and a concomitant perturbation of the methionine ligand.
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PMID:A 1H-NMR longitudinal relaxation study of the interaction between cytochrome c and cytochrome c oxidase. 630 52

Histochemical studies on the activities of 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD), succinate dehydrogenase (SDH) and cytochrome oxidase (CY-O) in rabbit ovarian follicles at various times after the administration of hCG were performed to investigate the relationship between the activities of steroid biosynthesis and the respiratory system. The activities of 3 beta-HSD and SDH were studied by using the tetrazolium salt and CY-O activities by the method of Seligman with prefixation. On the granulosa cell layer prior to the administration of hCG, no activities of 3 beta-HSD and CY-O were detectable, while slight activities of SDH were observed. These three enzymes showed intense activities on the granulosa cell layer 3 hours after the administration of hCG, which were maintained till the time of ovulation. The results indicated that increased activities of steroid biosynthesis in the granulosa cell layer after LH-surge were accompanied by the accelerated TCA cycle and respiratory chain. Energy from accelerated glycolysis may be utilized for steroid biosynthesis in preovulatory granulosa cells. Increased O2 consumption due to accelerated aerobic glycolysis is in accordance with hyperactivity of perifollicular capillaries, which finally leads to rapid follicular expansion and ovulation.
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PMID:[A histochemical study of the respiratory system in rabbit ovarian follicles during ovulation]. 632 56

For the purpose of describing early chondrogenic metabolic and structural events, measurements were made of oxidative and other enzymatic activities at various stages in the morphologic development of chondrocytes over a period of 18 to 20 days in continuous cell culture. Comparisons were also made between cells grown in 20% O2 and in 35% O2. These cultures exhibited rapid confluence (within 24 hours), early development of cartilaginous nodules by Day 2 to 3 and metachromatic staining of the chondrocyte matrix by Day 3 to 4. Under 35% O2, cell sheets were thicker and there was increased pleomorphism of chondrocyte and fibroblast cell types, with a relative increase of fibroblast components and reduction in chondroblasts and chondrocyte aggregates. Using the von Kossa staining procedure, calcium salt deposition was observed by Day 9. There was no apparent difference in mineralization of cultures grown under the low and high O2 tensions. Under normoxic conditions cytochrome oxidase and malate dehydrogenase (MDH) activities increased rapidly for the first three to four days and then remained essentially constant. Lactate dehydrogenase (LDH) activity increased continuously over the life of the culture. Acid phosphatase increased rapidly until about Day 13 after which it remained constant, whereas alkaline phosphatase showed a bimodal activity profile. Under hyperoxic conditions, cytochrome oxidase, MDH and alkaline phosphatase activity were significantly inhibited. LDH and acid phosphatase activities were markedly inhibited initially but with time showed a degree of recovery.
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PMID:Development of chick limb bud chondrocytes in cell culture: morphologic and oxidative metabolic observations. 701 57

Dexamethasone and aldosterone are major activators of Na+ reabsorption in tight epithelia. The genes whose expression mediates the steroid actions are mostly unknown. To identify such genes, we performed differential screening of a rat colon cDNA library with total 32P-labeled cDNA probes reverse transcribed from steroid-stimulated and steroid-depleted poly(A)+ RNA. Several cDNAs whose corresponding mRNA is enhanced two- to threefold after dexamethasone injection were identified. Partial sequencing indicated that four of them code for subunits of cytochrome-c oxidase and 16S mitochondrial mRNA. The dexamethasone-induced increase in mitochondrial RNA abundance could not be mimicked by a low-salt diet, found to increase plasma aldosterone from 1.0 +/- 0.1 to 12.8 +/- 1.4 nM. Induction of mitochondrial genes by adrenal steroids may serve to prevent limitation of transport by the ATP supply to the Na(+)-K+ pump under conditions of maximal stimulation of Na+ transport.
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PMID:Dexamethasone enhances expression of mitochondrial oxidative phosphorylation genes in rat distal colon. 749 22

The Fv fragment of a monoclonal antibody, 7E2 (IgG1, kappa, murine), which is directed against the integral membrane protein cytochrome c oxidase (EC 1.9.3.1) from Paracoccus denitrificans, was cloned and produced in Escherichia coli. Crystals suitable for high-resolution X-ray analysis were obtained by microdialysis under low salt conditions. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit cell dimensions of a = 51.51 A, b = 56.15 A, c = 99.86 A (1 A = 0.1 nm) and contain one Fv fragment per asymmetric unit. Using synchrotron radiation diffraction data were collected up to 1.28 A resolution. This high resolution is very unusual for a heterodimeric protein. The crystals should open the way for refining not only the atomic positions, but also for obtaining information about internal dynamics.
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PMID:Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 A resolution. 771 72


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