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Cytochemical bioassay -- Validity -- Laboratory manuals. : Validation of cell-based assays in the GLP setting : a practical guide / edited by Uma Prabhakar and Marian Kelley  2008 1
  Cytochemistry -- 4 Related Subjects   4
Cytochemistry.   16
Brain -- Cytochemistry. : Androgenic activity and possible neuroendocrine actions of rat cerebellar astrocytes / Robert Gasperini  1995 1
Cytochemistry -- Congresses.   2
Fungi -- Cytochemistry : Fungal protoplast : a biotechnological tool / D. Lalithakumari  2019 1
Cytochemistry -- Handbooks, manuals, etc. : Handbook of cellular chemistry  1975 1
Cytochemistry -- Methodology.   3
Cytochemistry -- Periodicals   7
 

Cytochemistry Technique -- See Also the narrower term Cytofluorometry


  1
Cytochemistry -- Technique.   2
Tradescantia -- Cytochemistry. : Studies of natriuretic peptides in Tradescantia / I. Nengah Suwastika  1999 1
Trees -- Cytochemistry -- Technique. : Wood formation in trees : cell and molecular biology techniques / edited by Nigel Chaffey  2002 1
 

Cytochrome -- See Cytochromes


Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands
  1
Cytochrome b. : Type-B Cytochromes : Sensors and Switches / Jonathan L. Kiel  2018 1
Cytochrome-B(5) Reductase. : Cytochrome b5 reductase deficiency and hereditary methemoglobinemia / Josef T. Prchal  2007 1
Cytochrome-B(5) Reductase -- deficiency.   2
Cytochrome c Group. : Mitochondrial oxidative phosphorylation : nuclear-encoded genes, enzyme regulation, and pathophysiology / edited by Bernhard Kadenbach  2012 1
  Cytochrome P-450 -- 3 Related Subjects   3
Cytochrome P-450.   18
 

Cytochrome P-450 2E1 -- See Cytochrome P-450 CYP2E1


  1
 

Cytochrome P-450 (ALC) -- See Cytochrome P-450 CYP2E1


An ethanol-inducible cytochrome P450 enzyme that metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Substrates include ETHANOL; INHALATION ANESTHETICS; BENZENE; ACETAMINOPHEN and other low molecular weight compounds. CYP2E1 has been used as an enzyme marker in the study of alcohol abuse
  1
 

Cytochrome P-450 (Arom) -- See Aromatase


  1
Cytochrome P-450 -- Congresses. : Cytochrome P-450, biochemistry, biophysics, and environmental implications : proceedings of the 4th International Conference on Cytochrome P-450 held in Kuopio, Finland, May 31-June 3, 1982 / editors, Eino Hietanen, Matti Laitinen, Osmo Hänninen  1982 1
 

Cytochrome P-450 CYP19 -- See Aromatase


  1
Cytochrome P-450 CYP2B6. : CYP2 family / Ann K. Daly  2016 1
Cytochrome P-450 CYP2C19. : CYP2 family / Ann K. Daly  2016 1
Cytochrome P-450 CYP2C8. : CYP2 family / Ann K. Daly  2016 1
Cytochrome P-450 CYP2C9. : CYP2 family / Ann K. Daly  2016 1
Cytochrome P-450 CYP2D6.   2
Cytochrome P-450 CYP2E1.   2
Cytochrome P-450 CYP2E1 -- Metabolism. : Cytochrome P450 2E1 : its role in disease and drug metabolism / Aparajita Dey, editor  2013 1
Cytochrome P-450 CYP2E1 -- toxicity. : Cytochrome P450 2E1 : its role in disease and drug metabolism / Aparajita Dey, editor  2013 1
Cytochrome P-450 CYP2E1 -- Toxicology. : Cytochrome P450 2E1 : its role in disease and drug metabolism / Aparajita Dey, editor  2013 1
 

Cytochrome P-450-Dependent Monooxygenase -- See Cytochrome P-450 Enzyme System


A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism
  1
Cytochrome P-450 Enzyme System.   12
Cytochrome P-450 Enzyme System -- analysis. : Cytochrome P450. Part B / edited by Eric F. Johnson, Michael R. Waterman  1996 1
Cytochrome P-450 Enzyme System -- chemistry. : Cytochrome P450 : structure, mechanism, and biochemistry / edited by Paul R. Ortiz de Montellano  2005 1
Cytochrome P-450 Enzyme System -- genetics.   3
Cytochrome P-450 Enzyme System -- metabolism.   7
Cytochrome P-450 Enzyme System -- pharmacology. : CYP2D : genetics, pharmacology and clinical relevance / editor, Pierre Baumann  2014 1
Cytochrome P-450 Enzyme System -- physiology.   2
Cytochrome P-450 Enzyme System -- therapeutic use. : CYP2D : genetics, pharmacology and clinical relevance / editor, Pierre Baumann  2014 1
 

Cytochrome P-450 Enzymes -- See Cytochrome P-450 Enzyme System


A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism
  1
 

Cytochrome P-450 Families -- See Cytochrome P-450 Enzyme System


A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism
  1
Cytochrome P-450 -- Genetics. : CYP2D : genetics, pharmacology and clinical relevance / editor, Pierre Baumann  2014 1
 

Cytochrome P-450 IIE1 -- See Cytochrome P-450 CYP2E1


An ethanol-inducible cytochrome P450 enzyme that metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Substrates include ETHANOL; INHALATION ANESTHETICS; BENZENE; ACETAMINOPHEN and other low molecular weight compounds. CYP2E1 has been used as an enzyme marker in the study of alcohol abuse
  1
 

Cytochrome P-450-J -- See Cytochrome P-450 CYP2E1


An ethanol-inducible cytochrome P450 enzyme that metabolizes several precarcinogens, drugs, and solvents to reactive metabolites. Substrates include ETHANOL; INHALATION ANESTHETICS; BENZENE; ACETAMINOPHEN and other low molecular weight compounds. CYP2E1 has been used as an enzyme marker in the study of alcohol abuse
  1
Cytochrome P-450 -- Metabolism. : Cytochromes P450 : role in the metabolism and toxicity of drugs and other xenobiotics / edited by Costas Ioannides  2008 1
 

Cytochrome P-450 Monooxygenase -- See Cytochrome P-450 Enzyme System


A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism
  1
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