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	Cytochrome P-450
		The term CYTOCHROME P-450 refers to a group of enzymes with are located on the endoplasmic reticulum.
		It is know that the gene for cytochrome P-450 has existed for more then 3.5 billion years.
		The second table shows various drugs and the various cytochrome P-450 enzyme systems that either inhibit or induce that drugs metabolism.
	www.edhayes.com /startp450.html (323 words)

	Cytochrome - Wikipedia, the free encyclopedia
		Cytochromes are generally membrane-bound proteins that contain heme groups and carry out electron transport or catalyse reductive/oxidative reactions.
		Cytochromes are thus capable of performing oxidation and reduction.
		Because the cytochromes (as well as other complexes) are held within membranes in an organized way, the redox reactions are carried out in the proper sequence for maximum efficiency.
	en.wikipedia.org /wiki/Cytochrome (323 words)

	Cytochrome c oxidase (Site not responding. Last check: 2007-10-20)
		The enzyme cytochrome c oxidase (PDB [http://www.rcsb.org/pdb/cgi/explore.cgi?pid=85881034355622&page=0&pdbId=2OCC 2OCC], EC 1.9.3.1) is a large transmembrane protein found in the mitochondrion and is the terminal electron acceptor in the electron transfer chain, taking 4 reducing equivalents from cytochrome c and converting molecular oxygen to water.
		Cytochrome P450 Identification of a novel transcriptional silencer in the protein-coding region of the human cytochrome P450 2C9 gene.
		Cytochrome P450 Reductase Overview of the biology, enzymology, and structure of cytochrome P450 reductase, an unusual electron transfer flavoprotein.
	www.serebella.com /encyclopedia/article-Cytochrome_c_oxidase.html (420 words)

	Cytochrome
		Nitrobacter winogradskyi cytochrome a1c1 is an iron-sulfur molybdoenzyme having hemes a and c.
		The fluorescence spectra of the molybdenum cofactor derivative prepared from cytochrome a1c1 were very similar to those of the cofactor derivative from xanthine oxidase, and the aponitrate reductase of nit-1 mutant of Neurospora crassa was complemented by addition of the molybdenum cofactor derived from the cytochrome.
		The content of cytochrome a1 in the cells cultivated with the medium in which tungsten was substituted for molybdenum markedly decreased as compared with that in the cells cultivated in the molybdenum-supplemented medium.
	www.ithyroid.com /cytochrome.htm (1736 words)

	Coenzyme Q - cytochrome c reductase - Wikipedia, the free encyclopedia
		It is a transmembrane lipoprotein, and it catalyzes the reduction of cytochrome c by accepting reducing equivalents from Coenzyme Q (CoQ):
		The major prosthetic groups in the complex are a pair of cytochromes, the b cytochrome and the c
		The toxic antimycin-A inhibits the transfer of electrons from Complex III to Complex IV (Cytochrome c oxidase).
	en.wikipedia.org /wiki/Coenzyme_Q_-_cytochrome_c_reductase (223 words)

	Cytochrome P450 oxidase - Wikipedia, the free encyclopedia (Site not responding. Last check: 2007-10-20)
		Cytochrome P450 oxidase (commonly abbreviated CYP) is a generic term for a large number of related, but distinct, oxidative enzymes (EC 1.14) important in animal physiology.
		Cytochrome P450 sequence homologs have been determined in all lineages of life, including mammals, birds, fish, insects, worms, sea squirts, sea urchins, plants, fungi, slime molds, bacteria and archaea.
		Cytochromes P450 are present in many other tissues of the body including the mucosa of the gastrointestinal tract, and play important roles in hormone synthesis and breakdown (including estrogen and testosterone synthesis and metabolism), cholesterol synthesis, and vitamin D metabolism.
	www.marijuana.com /wiki/Cytochrome_P450 (811 words)

	cytochrome on Encyclopedia.com
		CYTOCHROME [cytochrome], protein containing heme (see coenzyme) that participates in the phase of biochemical respiration called oxidative phosphorylation.
		Cytochromes act as carriers of hydride ions (sometimes considered to be the equivalent of electron pairs) in the series of complex enzymes known as the electron transport chain.
		Synergistic embryotoxicity of polycyclic aromatic hydrocarbon aryl hydrocarbon receptor agonists with cytochrome p4501a inhibitors in fundulus heteroclitus.(Research)
	www.encyclopedia.com /html/c1/cytochro.asp (411 words)

	Cytochrome C ELISA Kit: APT200
		Cytochrome c functions in the respiratory chain by interacting with redox partners of complex III and complex IV (Hatefi 1985; Mathews 1985).
		Cytochrome c participates in the formation of a cytosolic complex which is composed of cytochrome c itself (Apaf-2, 15 kDa), Apoptosis protease-activating factor (Apaf-1, 130 kDa) and caspase-9 (Apaf-3, 46 kDa).
		Cytochrome c present in the sample or standard binds to the antibodies adsorbed on the plate; a biotin-conjugated monoclonal anti-cytochrome c antibody is added and binds to cytochrome c captured by the first antibody.
	www.chemicon.com /Product/ProductDataSheet.asp?ProductItem=APT200 (632 words)

	Chapter 4 - Cytochrome c
		I is NADH dehydrogenase, II is succinate dehydrogenase, C is cytochrome c, Fo and F1 belong to the ATPase, cytochrome c oxidase is shown where oxygen is reacting, and cytochrome c reductase is between II and cytochrome c oxidase.
		Cytochrome c is reduced by cytochrome c reductase on the outer face of the cytosolic side of the inner membrane.
		Cytochrome c is easily separated from its mitochondrial environment because of its solubility in water.
	www.phattimes.com /myoglobin/chapter4.htm (1609 words)

	Cytochrome C antibody (ab6400) datasheet (Site not responding. Last check: 2007-10-20)
		Cytochrome C is an electron transporting protein that resides within the intermembrane space of the mitochondria, where it plays a critical role in the process of oxidative phosphorylation and production of cellular ATP.
		Following exposure to apoptotic stimuli, cytochrome C is rapidly released from the mitochondria into the cytosol, an event which may be required for the completion of apoptosis in some systems.
		Cytosolic cytochrome C functions in the activation of caspase 3, an ICE family molecule that is a key effector of apoptosis.
	www.abcam.com /?datasheet=6400 (552 words)

	Margaret Wong-Riley, PhD
		Cytochrome oxidase as a metabolic marker for neuronal activity.
		Since cytochrome oxidase is a highly sensitive marker of neuronal activity, we are investigating its mechanism of regulation in the brain.
		Cytochrome oxidase is one of only four proteins in mammalian cells that are bigenomically encoded.
	www.mcw.edu /cellbio/bios/wong-riley.html (816 words)

	Cytochrome c oxidase (Site not responding. Last check: 2007-10-20)
		Cytochrome c oxidase plays a vital role in oxidative phosphorylation: it is where the electrons reach their final acceptor.
		The importance of cytochrome c oxidase is its role as a thermodynamic force for oxidative phosphorylation and its ability to contain dangerous partially reduced intermediates, superoxides, which can cause genetic and tissue damage.
		Cytochrome c oxidase also affects aggregation of beta amyloid peptide which leads to plaque in the brain which is associated with the Alzheimer's disease.
	www.chem.uwec.edu /Chem406_F97/Webpages97/jscott/cco2.html (1390 words)

	CE: Cytochrome P450 Enzymes
		The term "cytochrome P450" refers to a group of enzymes that are responsible for, among other things, the metabolism of many of the drugs in use today.
		Drugs that inhibit a certain cytochrome P450 enzyme are not necessarily metabolized by that enzyme, and by the same token, drugs that are metabolized by an enzyme do not necessarily inhibit that enzyme.
		The cytochrome P450 enzymes are the most important drug-metabolizing enzymes in humans, and as such, play a major role in many drug-drug and drug-food interactions.
	www.geocities.com /hupiteekki/paihde01.htm (2936 words)

	Sublobular Distribution Of Cytochromes In Cold-Stored Rat Liver (Site not responding. Last check: 2007-10-20)
		A comparison is made between images of oxidized and reduced mitochondrial cytochrome a and cytochrome c in coupled and uncoupled (dinitrophenol) cold-stored liver during transitions in oxygen delivery.
		Cytochrome a difference images for air to nitrogen transitions produced reflectance changes that were 63% as large as those for oxygen to nitrogen transitions.
		Periportal to pericentral differences are more pronounced from cytochrome a as compared to cytochrome c in uncoupled livers as well as coupled livers, but a marked difference exists between the behavior of cytochrome c in coupled and uncoupled livers.
	www.evergreen.edu /biophysics/papers/ISOTT_liver.htm (449 words)

	29+ Evidences for Macroevolution: Part 4
		Cytochrome c is an essential and ubiquitous protein found in all organisms, including eukaryotes and bacteria (Voet and Voet 1995, p.
		Cytochrome c is an extremely functionally redundant protein, because many dissimilar sequences all form cytochrome c electron transport proteins.
		In fact, the cytochrome c genes from tuna (fish), pigeon (bird), horse (mammal), Drosophila fly (insect), and rat (mammal) all function in yeast that lack their own native yeast cytochrome c (Clements et al.
	www.talkorigins.org /faqs/comdesc/section4.html (5370 words)

	anti-Cytochrome c, FITC Conjugated CytoLight(TM) Kit > Assay Designs (Site not responding. Last check: 2007-10-20)
		Cytochrome c, ~13 kDa and 105 amino acids long, is a nuclear-encoded component of the mitochondrial respiratory chain that is imported as an apoenzyme into mitochondria, where it is converted to the mature form by the addition of a heme group.
		In addition to its role in oxidative phosphorylation, the release of Cytochrome c from the mitochondrial intermembrane space to the cytosol results in nuclear apoptosis.
		Binding of APAF1 to Cytochrome c allows APAF1 to form a ternary complex with and activate the initiator Procaspase-9 in the presence of dATP.
	www.assaydesigns.com /products/catalog/detection_kits/product_FITC_Cytochrome_c.htm (413 words)

	Cytochrome c peroxidase - Wikipedia, the free encyclopedia (Site not responding. Last check: 2007-10-20)
		Cytochrome c peroxidase, or CCP (PDB 2CYP, EC 1.11.1.5) is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome c and reduces hydrogen peroxide to water:
		Cytochrome c peroxidase can react with hydroperoxides other than hydrogen peroxide, but the reaction rate is much slower than with hydrogen peroxide.
		It was first isolated from baker's yeast by R. Altschul, Abrams, and Hogness in 1940, though not to purity.
	www.sciencedaily.com /encyclopedia/cytochrome_c_peroxidase (297 words)

	HDCN-- Drug Alerts: Cisapride/cytochrome P450 (Site not responding. Last check: 2007-10-20)
		Cytochrome P-450 is a superfamily of more than 100 enzymes catalyzing a large number of bioactivation and detoxication reactions.
		The large number of different cytochrome enzymes and genetic polymorphism in the activity of these enzymes complicates the use of drugs metabolized by them.
		Cytochrome P-450 IIIA, one of the cytochrome enzymes, is inhibited by ketoconazole, itraconazole, miconazole, troleandomycin, erythromycin, fluconazole, and clarithromycin.
	www.hdcn.com /misc/da510cis.htm (451 words)

	Cytochrome p450
		Oxidative metabolism by cytochrome p450 enzymes is a primary method of drug metabolism.
		Drug interactions involving the cytochrome p450 system are common, and generally result from either enzyme inhibition or induction.
		Cytochrome p450 enzymes are often designated by the letters CYP followed by a set of letters and numbers that distinguish enzyme isoforms.
	www.hospitalist.net /highligh.htm (494 words)

	Altered Cytochrome c Display Precedes Apoptotic Cell Death in Drosophila -- Varkey et al. 144 (4): 701 -- The Journal ...
		Cytochrome c in the total cell lysates (lanes 1-3), heavy membrane fractions (lanes 4-6), and S-100 cytosol (lanes 7-9) was visualized by Western blot analyses using mAb 7H8.
		Note that cytochrome c efflux into the cytosol of apoptotic cells was not observed, and that cytochrome c was substantially enriched in heavy membrane fractions which contain mitochondria.
		Altered cytochrome c display is provoked by expression of the apoptosis activators, rpr or grim.
	www.jcb.org /cgi/content/full/144/4/701 (6594 words)

	Cytochrome C
		Cytochrome C is a protein found in almost all living things.
		It happens that the cytochrome C in humans is slightly different from the cytochrome C in bacteria, but it still functions the same way.
		He showed, for example, that the cytochrome C in bacteria is 64% different from horses and pigeons, 65% different from tuna and silkmoths, 66% different from wheat, and 69% different from yeast.
	www.scienceagainstevolution.org /v7i10f.htm (1372 words)

	Cytochrome P450 Proteins and Potential Utilization in Biodegradation (Site not responding. Last check: 2007-10-20)
		The cytochrome P450 enzymes are major catalysts involved in the oxidations of xenobiotic chemicals in microorganisms as well as higher animals and plants.
		The cytochrome P450 enzymes are spread through the phylogenetic spectrum and, collectively, are major catalysts involved in the aerobic oxidation of almost all classes of organic molecules (for a recent review, see the entire January 1992 issue of FASEB J).
		Nucleotide sequence of the Pseudomonas putida cytochrome P-450cam gene and its expression in Escherichia coli.
	www.ehponline.org /members/1995/Suppl-5/guengerich-full.html (2358 words)

	Cytochrome c release into cytosol with subsequent caspase activation during warm ischemia in rat liver -- Soeda et al. ...
		C: cytochrome c in the cytosolic fraction during ischemia and reperfusion was quantified by ELISA.
		Cytochrome c and cytochrome oxidase subunit IV immunostaining of control liver and liver subjected to 90 min of ischemia.
		Cytochrome c immunostaining of the liver subjected to 90 min of ischemia viewed at lower magnification (original magnification, ×100) is shown in C.
	ajpgi.physiology.org /cgi/content/full/281/4/G1115 (4954 words)

	Mutations in the membrane anchor of yeast cytochrome c1 compensate for the absence of Oxa1p and generate ... (Site not responding. Last check: 2007-10-20)
		Mutations in the membrane anchor of yeast cytochrome c1 compensate for the absence of Oxa1p and generate carbonate-extractable forms of cytochrome c1.
		The suppressor mutations correspond to various amino acid substitutions, all located in the membrane anchor of cytochrome c1 and we have shown that in addition to membrane-bound cytochrome c1, fast-migrating carbonate-extractable forms accumulate in all the suppressor strains.
		The cytochrome c1 double mutant still retains the suppressor activity suggesting that the suppressor function is independent of the electron transfer activity.
	www.yeastgenome.org /yeast98/abshtml/184.html (328 words)

	cytochrome c oxidase and senescence (Site not responding. Last check: 2007-10-20)
		Intron alpha is the first intron of the cytochrome c oxidase subunit I gene (COX1).
		We describe here the first mutant of P. anserina that has the alpha sequence precisely deleted and whose cytochrome c oxidase activity is identical to that of wild-type cells.
		A comparison was made among five different species of dipteran flies, namely, Drosophila melanogaster (fruit fly), Musca domestica (house fly), Sarcophaga bullata (flesh fly), Calliphora vicina (blow fly) and Phaenecia sericata (a species of blow flies), which range more than 2-fold in their life span potentials.
	www.cryonet.org /cgi-bin/dsp.cgi?msg=13378 (498 words)

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