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  • cytochrome P-450 system
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  • cytochrome
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  • cytochrome
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  • cytochrome
    ½ÃÅäÅ©·Ò
  • cytochrome oxidase test
    ½ÃÅäÅ©·Ò»êÈ­È¿¼Ò°Ë»ç
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  • Cytochrome
    ½ÃÅäÅ©·Ò, »çÀÌÅäÅ©·Ò
  • NADH-cytochrome b5 reductase
    NADH-½ÃÅäÅ©·Òb5¸®´öŸ¾ÆÁ¦
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  • cytochrome P-450
    »çÀÌÅäÅ©·Ò P-450 <<(µ¿½Ä¹°ÁßÀÇ) È£Èí»ö¼Ò>
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  • cytochrome p450
    ½ÃƮũ·Ò p 450
  • cytochrome
    »çÀÌÅ©·Ò.
  • cytochrome C oxidase deficiency
    ½ÃƮũ·Ò C ¿Á½Ã´ÙÁ¦(»êÈ­È¿¼Ò)°áÇÌ
  • cytochrome b5 reductase deficiency
    ½ÃÅäÅ©·Ò b5 ȯ¿øÈ¿¼Ò °áÇÌ
  • cytochrome oxidase
    »çÀÌÅäÅ©·Ò ¿Á½Ãµ¥À̽º, »êÈ­È¿¼Ò(ß«ûùý£áÈ) .
  • cytochrome oxidase
    »çÀÌÅäÅ©·Ò»êÈ­¿ä¼Ò
  • cytochrome oxidase test
    »çÀÌÅäÅ©·Ò »êÈ­È¿¼Ò °Ë»ç
  • cytochrome reductase
    ½ÃÅäÅ©·Ò ·¹´ÚŸÁ¦<ȯ¿øÈ¿¼Ò(ü½êªý£áÈ)>.
  • cytochrome system
    ½ÃÅäÅ©·Ò ½Ã½ºÅÛ<Åë>.
  • oxidase test, (cytochrome)
    »êÈ­È¿¼Ò½ÃÇè (½ÃÅäÅ©·ÒÀÇ)
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  • cytochrome P450
    »çÀÌÅäÅ©·Ò P450
  • P450
    (ÑÀûÜ) »çÀÌÅäÅ©·Ò P450
  • coenzyme Q-cytochrome c reductase complex
    º¸È¿¼Ò(ÜÍý£áÈ) Q¡¤»çÀÌÅäÅ©·Ò C ¸®´ÚÅ×À̽º (ÔÒ) complex III
  • cytochrome
    »çÀÌÅäÅ©·Ò
  • cytochrome a
    »çÀÌÅäÅ©·Ò a
  • cytochrome b
    »çÀÌÅäÅ©·Ò b
  • cytochrome c
    »çÀÌÅäÅ©·Ò c
  • cytochrome c'
    "»çÀÌÅäÅ©·Ò c' (ÔÒ)RHP cytochrome,"
  • cytochrome c oxidase complex
    »çÀÌÅäÅ©·Ò c ¿Á½Ãµ¥À̽º º¹ÇÕü(ÜÜùêô÷) (ÔÒ) complex IV
  • cytochrome c : oxygen oxidoreductase
    »çÀÌÅäÅ©·Ò c »ê¼Ò(ß«áÈ) ¿Á½Ãµµ¸®´öÅ×À̽º (ÔÒ) complex IV
  • cytochrome d
    »çÀÌÅäÅ©·Ò d
  • cytochrome oxidase
    »çÀÌÅäÅ©·Ò ¿Á½Ãµ¥À̽º
  • RHP cytochrome
    RHP »çÀÌÅäÅ©·Ò
  • ubiquinol : cytochrome C oxidase
    À¯ºñÄû³î:»çÀÌÅäÅ©·Ò C ¿Á½Ãµ¥À̽º
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CCO cytochrome C oxidase
COX cytochrome c oxidase
CYC cyclophosphamide; cytochrome C
CYT cytochrome
cyt cytochrome; cytology, cytological; cytoplasm, cytoplasm
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CP450 Cytochrome P450
CYP450 Cytochrome P450
CYP1B1 Cytochrome P450 1B1
CYP2A6 Cytochrome P450 2A6
CYP2C19 Cytochrome P450 2C19
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  • cytochrome oxidase test
    »çÀÌÅäÅ©·Ò »êÈ­ È¿¼Ò °Ë»ç
  • mitochondrial cytochrome
    ¹ÌÅäÄܵ帮¾Æ¼º Ä¡ÅäÅ©·Ò
CancerWEB ¿µ¿µ ÀÇÇлçÀü ¸ÂÃã °Ë»ö °á°ú : 10 ÆäÀÌÁö: 1
cytochrome p-450 <biochemistry> Enzymes of the electron transport chain that are pigmented by virtue of their haem prosthetic groups.
They are highly conserved isozymes which are key components of the mixed-function oxidase system responsible for the biotransformation of many foreign compounds to mutagens and carcinogens.
Most mammals have several distantly related phenobarbital-inducible gene subfamilies.
(21 Jun 2000)
cytochrome p-450 cyp11b2 <enzyme> A multifunctional enzyme that catalyses the conversion of corticosterone to 18-hydroxycorticosterone and the subsequent conversion of 18-hydroxycorticosterone to aldosterone.
Registry number: EC 1.14.99.-
(12 Dec 1998)
cytochrome p-450 cyp1a1 <enzyme> A cytochrome p-450 enzyme capable of activating procarcinogenic polycyclic hydrocarbons and halogenated aromatic hydrocarbons into mutagenic compounds. Ethoxyresorufin acts as a substrate for cyp1a1 and measurement of ethoxyresorufin o-deethylase provides a more direct method of detection for this enzyme.
Registry number: EC 1.-
(12 Dec 1998)
cytochrome p-450 cyp1a2 <enzyme> A polycyclic aromatic hydrocarbon-inducible cytochrome which is of significant clinical interest due to the large number of drug interactions associated with induction and inhibition of theophylline. Caffeine is considered to be a model substrate for this enzyme. It also metabolises theophylline and antipyrene. Environmental factors including cigarette smoking, charbroiled meat, cruciferous vegetables, and a number of drugs including phenytoin, phenobarbital, and omeprazole produce increases in cyp1a2 activity.
Registry number: EC 1.-
(12 Dec 1998)
cytochrome p-450 cyp2b1 <enzyme> A major cytochrome p-450 enzyme which is inducible by phenobarbital in both the liver and small intestine. It is active in the metabolism of compounds like pentoxyresorufin, testosterone, and androstenedione. Cyp2b1 also mediates the activation of cyclophosphamide and ifosfamide to mutagens.
Registry number: EC 1.-
(12 Dec 1998)
cytochrome p-450 cyp2d6 <enzyme> A polymorphic enzyme that catalyses the hydroxylation of debrisoquine. It also metabolises several antidepressants and neuroleptics. This enzyme is deficient in up to 10 percent of the population.
Registry number: EC 1.14.99.-
(12 Dec 1998)
cytochrome p-450 cyp2e1 <enzyme> A polymorphic enzyme that activates carcinogenic n-nitrosamines, benzene, urethane, and other low molecular weight compounds. It is inducible by ethanol and metabilises alcohol. Experimentally, it is used to study the effects of ethanol usage and withdrawal via enzyme markers such as n-nitrosodimethylamine demethylase.
Registry number: EC 1.5.99.-
(12 Dec 1998)
cytochrome P-450 oxidase <enzyme> Oxidises NADPH with formation of hydrogen peroxide
Registry number: EC 1.6.2.-
Synonym: NADPH-p450 reductase, NADPH-cytochrome p450 reductase, cytochrome p450 reductase, cpra gene product
(26 Jun 1999)
cytochrome P-450-dependent digitoxin 12beta-hydroxylase <enzyme> Isolated from digitalis lantata cell cultures
Registry number: EC 1.14.99.-
Synonym: digitoxin 12beta-hydroxylase
(26 Jun 1999)
cytochrome P-450SCC Cholesterol monooxygenase (side chain cleaving).
Origin: 450 nm, the absorption maximum that the CO compound of the reduced pigment exhibits
(05 Mar 2000)
CancerWEB ¿µ¿µ ÀÇÇлçÀü À¯»ç °Ë»ö °á°ú : 15 ÆäÀÌÁö: 1
core II protein, ubiquinol-cytochrome c reductase <chemical> Member of the mitochondrial-protein-processing family; protein found in subunits of ubiquinol-cytochrome c reductase; amino acid sequence given in first source
Synonym: core II protein, uccreductase
(26 Jun 1999)
core I protein, ubiquinol-cytochrome c reductase <chemical> Member of the mitochondrial-protein-processing family; protein found in subunits of ubiquinol-cytochrome c reductase; amino acid sequence given in first source
Synonym: core I protein, uccreductase
(26 Jun 1999)
porphyrin cytochrome c peroxidase <enzyme> From yeast; haem group of cytochrome c peroxidase (EC 1.11.1.5) replaced by protoporphyrin ix
Registry number: EC 1.11.1.-
Synonym: pcc-peroxidase
(26 Jun 1999)
cytochrome <biochemistry> Any electron transfer haemoprotein having a mode of action in which the transfer of a single electron is effected by a reversible valence change of the central iron atom of the haem prosthetic group between the +2 and +3 oxidation states.
Classified as cytochromes a in which the haem contains a formyl side chain, cytochromes b, which contain protohaem or a closely similar haem that is not covalently bound to the protein, cytochromes C in which protohaem or other haem is covalently bound to the protein and cytochromes d in which the iron tetrapyrrole has fewer conjugated double bonds than the haems have. Well known cytochromes have been numbered consecutively within groups and are designated by subscripts (beginning with no subscript), for example cytochromes C, c1, C2,. New cytochromes are named according to the wavelength in nanometres of the absorption maximum of the a band of the iron (II) form in pyridine, for example, C 555.
Origin: Gr. Chroma = colour
(18 Nov 1997)
cytochrome a <chemical> Cytochromes (electron-transporting proteins) in which the haem prosthetic group is haem a, i.e., the iron chelate of cytoporphyrin ix.
Chemical name: Cytochrome a
(12 Dec 1998)
cytochrome aa3 <enzyme> An enzyme complex of the inner mitochondrial membrane that catalyses the reaction between ferrocytochrome c and oxygen to yield ferricytochrome c and water.
It is associated with the pumping of protons and the resultant phosphorylation of ADP to ATP. The reaction is the terminal event in the electron transport scheme by which oxygen is used for fuel combustion. It is a part of Complex IV of the respiratory chain.
A deficiency of one or more of the polypeptides of this complex results in neuronal loss in brain leading to psychomotor retardation and neurodegenerative disease.
Synonym: cytochrome aa3, indophenol oxidase, indophenolase. Chemical name: Ferricytochrome-c:oxygen oxidoreductase
Registry number: EC 1.9.3.1
(12 Dec 1998)
cytochrome b <chemical> Cytochromes (electron-transporting proteins) with protoheme or a related haem as the prosthetic group. The prosthetic group is not covalently bound to the protein moiety.
Chemical name: Cytochrome b
(12 Dec 1998)
cytochrome b5 <chemical> A cytochrome occurring in the endoplasmic reticulum that acts as an intermediate electron carrier in some reactions catalyzed by mixed function oxidases, e.g., fatty acid desaturation. It further activates molecular oxygen for an attack on the substrate. Mw 16kda.
Chemical name: Cytochrome b5
(12 Dec 1998)
cytochrome b5 reductase <enzyme> An enzyme catalyzing the reduction of 2ferricytochrome b5 to 2ferrocytochrome b5 at the expense of NADH; has a role in fatty acid desaturation; a deficiency can lead to hereditary methemoglobinaemia (type I, only observed in erythrocyte cytosol; type II, deficiency in all tissues; type III, deficiency in all haematopoetic cells).
(05 Mar 2000)
cytochrome b(5) reductase <enzyme> May be the enzyme for methemoglobin reductase activity
Registry number: EC 1.6.2.2
Synonym: NADH-cytochrome b5 reductase, mcr1 protein, saccharomyces cerevisiae, mcr1 gene product
(26 Jun 1999)
cytochrome C A type of cytochrome, a protein which carries electrons, that is central to the process of respiration in mitochondria (an organelle found in eukaryotes which produces energy).
(09 Oct 1997)
cytochrome c1 <chemical> The 30-kD membrane-bound c-type protein of mitochondria that functions as an electron donor to cytochrome c in the mitochondrial and bacterial respiratory chain.
Chemical name: Cytochrome c1
(12 Dec 1998)
cytochrome C1 haem lyase <enzyme> A mitochondrial haem lyase from saccharomyces cerevisiae; mw about 31 kD; facilitates covalent attachment of haem to the apoforms of c-type cytochromes
Registry number: EC 4.99.-
Synonym: yeast cc1hl
(26 Jun 1999)
cytochrome c2 reductase <enzyme> An enzyme catalyzing the reduction of 2 ferricytochrome c2 to 2 ferrocytochrome c2 at the expense of NADPH.
Synonym: cytochrome c2 reductase.
(05 Mar 2000)
cytochrome c3 hydrogenase A hydrogenase enzyme catalyzing reduction of 2ferricytochrome c3 by H2 to 2ferrocytochrome c3 and 2H+.
(05 Mar 2000)
MeSH(Medical Subject Headings) ¸ÂÃã °Ë»ö (http://www.nlm.nih.gov) °á°ú : 5 ÆäÀÌÁö: 1
  • Cytochrome P-450 CYP1A1 - »õâ A liver microsomal cytochrome P-450 monooxygenase capable of biotransforming xenobiotics such as polycyclic hydrocarbons and halogenated aromatic hydrocarbons into carcinogenic or mutagenic compounds. They have been found in mammals and fish. This enzyme, encoded by CYP1A1 gene, can be measured by using ethoxyresorufin as a substrate for the ethoxyresorufin O-deethylase activity.
    Synonyms : 7-Ethoxyresorufin O-Deethylase, CYP 1A1, CYP1A1 Protein, Cytochrome P450 IA1, Ethoxyresorufin Dealkylase, Ethylresorufin O-Deethylase, Cytochrome P 450 CYP1A1
  • Cytochrome P-450 CYP1A2 - »õâ A cytochrome P-450 monooxygenase that can be induced by polycyclic aromatic xenobiotics in the liver of human and several animal species. This enzyme is of significant clinical interest due to the large number of drug interactions associated with its induction and its metabolism of THEOPHYLLINE. Caffeine is considered to be a model substrate for this enzyme. CYP1A2 activity can also be increased by environmental factors such as cigarette smoking, charbroiled meat, cruciferous vegetables, and a number of drugs including phenytoin, phenobarbital, and omeprazole.
    Synonyms : CYP 1A2, Caffeine Demethylase, Cytochrome P-450 LM(4), Cytochrome P-450 LM4, Cytochrome P-450d, Cytochrome P450 1A2, CYP1A2, Cytochrome P-450, Cytochrome P 450 CYP1A2, Cytochrome P 450d, Demethylase, Caffeine, O-Dealkylase, Phenacetin, Phenacetin O Dealkylase
  • Cytochrome P-450 CYP27A1 - »õâ An NAPH-dependent cytochrome P450 enzyme that catalyzes the oxidation of the side chain of sterol intermediates such as the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha, 12-alpha-triol. Cytochrome P-450 CYP27A1 is a mitochondrial enzyme; however microsomal-derived homologs of the enzyme have been identified and are included under this heading.
    Synonyms : 5-beta-Cholestane-3-alpha, 7-alpha, 12-alpha-triol 27-Hydroxylase, C27-Steroid 26-Hydroxylase, Cholestanetriol 26-Monooxygenase, Cytochrome P-450 CYP2R1, Cytochrome P-450 Steroid 27-Hydroxylase, Cytochrome P-450 Sterol 26-Hydroxylase, Cytochrome P450 2R1
  • Cytochrome P-450 CYP2B1 - »õâ A major cytochrome P-450 enzyme which is inducible by PHENOBARBITAL in both the LIVER and SMALL INTESTINE. It is active in the metabolism of compounds like pentoxyresorufin, TESTOSTERONE, and ANDROSTENEDIONE. This enzyme, encoded by CYP2B1 gene, also mediates the activation of CYCLOPHOSPHAMIDE and IFOSFAMIDE to MUTAGENS.
    Synonyms : 7-Benzyloxyresorufin O-Dealkylase, 7-Pentylresorufin O-Depentylase, CYP 2B1, Cytochrome P450 2B1, 7 Benzyloxyresorufin O Dealkylase, 7 Pentylresorufin O Depentylase, Benzyloxyresorufin O Dealkylase, Cytochrome P 450 CYP2B1, O-Dealkylase, Pentoxyresorufin
  • Cytochrome P-450 CYP2D6 - »õâ A cytochrome P450 enzyme that catalyzes the hydroxylation of many drugs and environmental chemicals, such as DEBRISOQUINE; ADRENERGIC RECEPTOR ANTAGONISTS; and TRICYCLIC ANTIDEPRESSANTS. This enzyme is deficient in up to 10 percent of the Caucasian population.
    Synonyms : CYP 2D6, Cytochrome P450 2D6, Debrisoquine 4-Monooxygenase, Imipramine 2-Hydroxylase, Sparteine Monooxygenase, 2-Hydroxylase, Imipramine, 4-Hydroxylase, Debrisoquine, 4-Monooxygenase, Debrisoquine, CYP2D6, Cytochrome P-450, Cytochrome P 450 CYP2D6
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cytochrome P-450 an enzyme that plays an important role in the metabolism of drugs and toxins in the liver. It also plays a role in the synthesis (formation) of steroid hormones in the adrenal cortex.
Ãâó: www.nutrabio.com/Definitions/definitions_c.htm
cytochrome P-450 This is a haem-containing protein which takes part in the phase I reactions of xenobiotics during biotransformation processes.
Ãâó: www.bio.hw.ac.uk/edintox/glossall.htm
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